Abstract
This chapter has two objects. The first is to outline the role of mineral elements in the activation of enzyme systems occurring in higher plants and microorganisms. The second is to discuss related aspects of interest to physiologists including multiple metal activation, status of essential and non-essential elements and effects of total metal content on enzyme patterns. It is necessary at times to refer to enzymes in animal tissues to illustrate certain points. References to many physiological studies in plant nutrition have been omitted where they do not directly concern aspects of enzyme activity. Reviews by Mulder (1950), Hewitt (1951) and Pirson (1955) deal with such related physiological aspects of mineral nutrition not included here. It is a pleasure to acknowledge the stimulation gained from reviews in the Annual Reviews of Biochemistry and Plant Physiology and especially from those of Mc Elroy (1953), Mc Elroy and Nason (1954), and the recent symposia of the McCollum-Pratt Institute (Johns Hopkins University Press, Baltimore) on Copper Metabolism (1950), on Phosphorus Metabolism (1951) on the Mechanism of Enzyme Action (1954), and on Inorganic Nitrogen Metabolism (1956), all edited by Mc Elroy and Glass.
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Literature
Adler, E., H. v. Euler, H. Gunther and M. Plass: Isocitric dehydrogenase and glutamic acid synthesis in animal tissues. Biochemic. J. 33, 1028–1045 (1939).
Agarwala, S. C.: Relation of nitrogen supply to the molybdenum requirements of cauliflower grown in sand culture. Nature (Lond.) 169, 1099–1100 (1952).
Agarwala, S. C., and E. J. Hewitt: Molybdenum as a plant nutrient. IV. The interrelationships of molybdenum and nitrogen supply in chlorophyll and ascorbic acid fractions in cauliflower plants grown in sand culture. J. Horticult. Sci. 29, 291–300 (1954).
Molybdenum as a plant nutrient. VI. Effects of molybdenum supply on the growth and composition of cauliflower plants given different sources of nitrogen supply in sand culture. J. Horticult. Sci. 30, 163–180 (1955).
Allen, M.B., and D. I. Arnon: Studies on nitrogen fixing bacteria. II. The sodium requirement of Anabaena cylindrica. Physiol. Plantarum (Copenh.) 8, 653–660 (1955a).
Studies on nitrogen fixing bacteria. I. Growth and nitrogen fixation by Anabaena cylindrica Lemm. Plant Physiol. 30, 366–372 (1955b).
Altmann, S. M., and E. M. Crook: Activation of enzymes by chelating agents. Nature (Lond.) 171, 76–77 (1953).
Altschul, A. M., R. Abrams and T. R. Hogness: Soluble cytochrome c peroxidase. J. of Biol. Chem. 130, 427–428 (1929).
Anderson, H. B.: The activation of Jack bean arginase by cobalt, manganese and iron. Biochemic. J. 39, 139–142 (1945).
Anderson, I. C., and H. J. Evans: Effect of manganese and certain other cations on isocitric dehydrogenase and malic enzyme activites in Phaseolus vulgaris. Plant Physiol. 31, 22–28 (1956).
Andreae, W. A.: The photoinduced oxidation of manganous ions. Arch. of Biochem. a. Biophysics. 55, 584–586 (1955).
Appleby, C. A., and R. K. Morton: Crystalline cytochrome and lactic dehydrogenase of yeast. Nature (Lond.) 173, 749–752 (1954).
Arnon, D. I.: Localisation of polyphenol oxidase in the chloroplasts of Beta vulgaris. Nature (Lond.) 162, 341–343 (1948).
Copper enzymes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris. Plant Physiol. 24, 1–15 (1949).
Criteria of essentiality of inorganic micronutrients for plants. Trace elements in plant physiology, pp. 31–39. Waltham, Mass.: Chronica Botanica 1950a.
Functional aspects of copper in plants. “Copper Metabolism”, pp. 89–114. Ed. W. D. Mc Elroy and B. Glass. Symposium. Baltimore: Johns Hopkins Univ. Press 1950b.
Extracellular photosynthetic reactions. Nature (Lond.)167, 1008–1011 (1951).
Growth and function as criteria in determining the essential nature of inorganic nutrients, chap. 13, pp. 313–341 in Univ. Wisconsin Centennial Symposium on mineral nutrition 1949. Ed. E. Truog, Madison (Wisconsin) 1952.
Arnon, D. I., A. Fujiwara, G. Wessel and J. T. Woolley: Molybdenum in the nutrition of Scenedesmus. Proe. Amer. Soe. Plant Physiol. Symposium, Madison 1953.
Arnon, D. I., and P. R. Stout: The essentiality of certain elements in minute quantity for plants with special reference to copper. Plant Physiol. 14, 371–375 (1939).
Arnon, D. I., and G. Wessel: Vanadium as an essential element for green plants. Nature (Lond.) 172, 1039–1041 (1953).
Arnon, D. I., F. R. Whatley and M. B. Allen: Photosynthesis by isolated chloroplasts. II. Photosynthetic phosphorylation, the conversion of light into phosphate bond energy. J. Amer. Chem. Soc. 76, 6324–6329 (1954).
Auhagen, E.: Über Co-carboxylase. Hoppe-Seylers Z. 209, 20–26 (1932).
Avis, P. G., F. Bergel and R. C. Bray: Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cows milk. J. Chem. Soc. Lond. 1955, 1100–1105.
Cellular constituents. The chemistry of xanthine oxidase. Part III. Estimations of the cofactors and the catalytic activities of enzyme fractions from cow’s milk. J. Chem. Soc. Lond. 1956, 1219–1226.
Avis, P. G., F. Bergel, R. C. Bray and K. V. Shooter: A crystalline material with xanthine oxidase activity. Nature (Lond.) 173, 1230–1231 (1954).
Baddiley, J.: Pyridoxal derivatives in transamination. Nature (Lond.) 170, 711–712 (1952).
Bailey, J. M., G. J. Thomas and W. J. Whelan: Selective inhibition of enzymic impurities associated with potato Phosphorylase. Biochemic. J. 49, Proc. VI (1951).
Bailey, K., and E. C. Webb: Purification and properties of yeast pyrophosphatase. Biochemic. J. 38, 394–398 (1944).
Purification of yeast hexokinase and its reaction with β.β-dichloro-diethyl sulphide. Biochemic. J. 42, 60–68 (1948).
Baker, D., and J. M. B. Nelson: Tyrosinase and plant respiration. J. Gen. Physiol. 26, 269–276 (1943).
Ballentine, R.: The biosynthesis of stable cobalto-proteins by plants. II. Interaction of iron and cobalt metabolism in Neurospora crassa. J. Cellul. a. Comp. Physiol. 42, 415–426 (1953).
Ballentine, R., and D. G. Stevens: The biosynthesis of stable cobalto-proteins by plants. J. Cellul. a. Comp. Physiol. 37, 369–388 (1951).
Bandurski, R. S., and C. M. Groines: Phospho-enolpyruvate carboxylase. Proc. Amer. Soc. Plant Physiol. Symposium, Madison (Wisconsin) 1953.
Bard, R. C., and I. C. Gunsalus: Glucose metabolism of Clostridium perfringens: Existence of a metallo-aldolase. J. Bacter. 59, 387–400 (1950).
Barker, H., A. H. Ennor and K. Harcourt: The catalytic effect of molybdate on the breakdown of phosphocreatine. Austral. J. Sci. Res. B 3, 337–345 (1950).
Barron, E. S. G., R. H. de Meio and E. Klemperer: Studies on biological oxidations. V. Copper and hemochromogens as catalysts for the oxidation of ascorbic acid. The mechanism of the oxidation. J. of Biol. Chem. 112, 625–640 (1936).
Baumann, E., and O. Schimke: d-Peptid-Spaltung durch Enzympräparate aus wachsenden Keimpflanzen. Beeinflussung durch natürliche und zusätzliche Aktivatoren. Zur Kenntnis der Peptidasen. II. Biochem. Z. 310, 119–130 (1941a).
d-Peptidase in wachsenden Teilen älterer Pflanzen. IV. Zur Kenntnis der Peptidasen. Biochem. Z. 310, 302–311 (1941b).
Beaudreau, G. S., and F. L. Renmert: Krebs cycle activity of particles from bean seedlings. Arch. of Biochem. a. Biophysics 55, 469–485 (1955).
Beevers, H., and W. O. James: The behaviour of secondary and tertiary amines in the presence of catechol and Belladonna catechol oxidase. Biochemic. J. 43, 636–639 (1948).
Beinert, H., and F. L. Crane: The function of electron transferring flavoprotein in the first oxidative step of the fatty acid cycle, pp. 601–624 in Symposium on Inorganic Nitrogen Metabolism, ed. by W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1956.
Berger, J., and G. S. Avery jr.: Glutamic and isocitric acid dehydrogenases in the Avena coleoptile. Amer. J. Bot. 31, 11–19 (1944).
Berger, J., and M. J. Johnson: Metal activation of peptidases. J. of Biol. Chem. 130, 641–654 (1939a).
The leucyl peptidases of malt, cabbage and spinach. J. of Biol. Chem. 130, 655–667 (1939b).
The action of dipeptidases. J. of Biol. Chem. 133, 639–640 (1940).
Berger, L., M. W. Slein, S. P. Colowick and C. F. Cori: Isolation of hexokinase from baker’s yeast. J. Gen. Physiol. 29, 379–391 (1946).
Bernheim, F.: The aldehyde oxidase of the potato. Biochemic. J. 22, 344–352 (1928).
Bertrand, D.: Études sur la laccase. II. Comparison avec les produits anterièrement decrits. Bull. Soc. Chim. biol. Paris 26, 40 (1944).
Études sur la laccase. VI. Remarques sur le sujet de la co-laccase. Bull. Soc. Chim. biol. Paris 29, 613–615 (1947).
Bertrand, G.: Sur l’intervention des manganèses dans les oxydations provoquées par la laccase. C. r. Acad. Sci. Paris 124, 1032–1035 (1897).
Bhagvat, K., and R. Hill: Cytochrome oxidase in higher plants. New Phytologist 50, 112–120 (1951).
Binkley, F., and M. Boyd: Catalytic cleavage of thio-amino acids. J. of Biol. Chem. 217, 67–77 (1955).
Black, S.: Yeast aldehyde dehydrogenase. Arch. of Biochem. a. Biophysics 34, 86–97 (1951).
Black, S., and N. G. Wright: β-aspartyl kinase and β-aspartyl phosphate. J. of Biol. Chem. 213, 27–37 (1955).
Boeri, E., E. Cutolo, M. Luzzati and L. Tosi: Preparation and properties of cytochrome b2 from yeast. Arch. of Biochem. a. Biophysics 56, 487–499 (1955).
Bonner, J.: Biochemical mechanisms in the respirations of the Avena coleoptile. Arch. of Biochem. 17, 311–326 (1948).
Bonner, J., and S. G. Wildman: Enzymatic mechanism on the respiration of spinach leaves. Arch. of Biochem. 10, 497–518 (1946).
Boroughs, H.: Studies on the acid phosphatases of green leaves. Arch. of Biochem. a. Biophysics 49, 30–42 (1954).
Bortels, H.: Weitere Untersuchungen über die Bedeutung von Molybdän, Vanadium, Wolfram und anderen Erdaschenstoffen für stickstoffverbindende und andere Mikroorganismen. Zbl. Bakter. 95, 193–218 (1936).
Über die Wirkung von Agar sowie Eisen, Molybdän und anderen Spurenelementen in stickstofffreier Nährlösung auf Azotobacter. Zbl. Bakter. 100, 373–393 (1939).
Bossard, M.: Action des molybdates sur divers enzymes. Bull. Soc. Chim. biol. Paris 29, 218–221 (1947).
Boswell, J. G.: Oxidation systems in the potato. Ann. of Bot., N. S. 9, 55–76 (1945).
Boswell, J. G., and G. C. Whiting: A study of the polyphenol oxidase system in potato tubers. Ann. of Bot., N.S. 2, 847–864 (1938).
Oxidase systems in the tissues of higher plants. New Phytologist 39, 241–265 (1940).
Bradfield, J. R. G.: Plant carbonic anhydrase. Nature (Lond.) 159, 467–468 (1947).
Brown, A. H., and D. R. Goddard: Cytochrome oxidase in wheat embryo. Amer. J. Bot. 28, 319–329 (1941).
Bucher, T.: Über ein phosphatübertragendes Gärungsferment. Biochim. et Biophysica Acta 1, 292–314 (1947).
Burk, D.: Azotase and nitrogenase in Azotobacter. Erg. Enzymforsch. 3, 23–57 (1934).
Burk, D., J. Hearson, L. Caroline and A. L. Shade: Reversible complexes of cobalt, histidine and oxygen gas. J. of Biol. Chem. 165, 723–724 (1946).
Burris, R. H.: Organic acids in plant metabolism. Annual Rev. Plant Physiol. 4, 91–114 (1953).
Calvin, M.: Chelation and catalysis. In: The Mechanism of Enzyme Action, pp. 221–244. Symposium McCollum Pratt Institute, ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1954.
Calvin, M., R. H. Bailes and W. K. Wilmarth: The oxygen carrying synthetic chelate compounds. I. J. Amer. Chem. Soc. 68, 2254–2256 (1946) et seq.
Caputto, R.: The enzymic synthesis of adenylic acid: adenosine kinase. J. of Biol. Chem. 189, 801–814 (1951).
Ceithamel, J., and B. Vennesland: The synthesis of tricarboxyhc acids by carbon dioxide fixation in parsley root preparations. J. of Biol. Chem. 178, 133–143 (1949).
Chance, B.: The state of catalase in the respiring bacterial cell. Science (Lancaster, Pa.) 116, 202–203 (1952).
Oxidase and peroxidase reactions in the presence of dihydroxymaleic acid. J. of Biol. Chem. 197, 577–589 (1952).
Chesters, C.G.C., and G. N. Rolinson: Trace elements and streptomycin production. J. Gen. Microbiol. 5, 559–565 (1951).
Cohen, P. P.: The carboxylase activity of Jack beans (Canavalia ensiformis) and soy beans (Glycine max.) J. of Biol. Chem. 164, 685–689 (1946).
Cohen, S. S.: Gluconokinase and the oxidative path of glucose-6-phosphate utilisation. J. of Biol. C hem. 189, 617–628 (1951).
Colter, J. S., and J. H. Quastel: Catalytic decomposition of hydroxylamine by haemoglobin. Arch. of Biochem. 27, 368–389 (1950).
Conn, E., B. Vennesland and L. M. Kraemer: Distribution of a triphosphopyridine nucleotide — specific enzyme catalysing the reversible oxidative decarboxylation of malic acid in higher plants. Arch. of Biochem. 23, 179–197 (1949).
Cori, G. T., S. P. Colowick and C. F. Cori: The enzymatic conversion of glucose-1-phosphoric ester to 6-ester in tissue extracts. J. of Biol. Chem. 124, 543–555 (1938).
Crane, F. L., J. G. Hange and H. Beinert: Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. et Biophysica Acta 17, 292–294 (1955).
Crewther, W. G.: Studies on Aerobacillus polymyxa. Austral. J. Biol. Sci. 6, 204–221 (1953).
Dalton, A. R., and J. M. Nelson: Tyrosinase from the wild mushroom, Lactarius piperatus. J. Amer. Chem. Soc. 61, 2946 (1939).
Damodaran, M., and T. R. Venkatesan: Amide synthesis in plants. I. The succinic oxidase system in plants. Proc. Indian Acad. Sci., Sect. B 13, 345–359 (1941).
Darken, M. A.: Production of vitamin B12 by microorganisms and its occurrence in plant tissues. Bot. Review 19, 99–130 (1953).
Davenport, H. E.: Cytochrome components in chloroplasts. Nature (Lond.) 170, 112–114 (1952).
Davenport, H. E., and R. Hill: The preparation and some properties of cytochrome f. Proc. Roy. Soc. Lond. Ser. B 139, 327–345 (1952).
Davies, D. R., and W. C. Davies: The colorimetric determination of phosphorus in the presence of interfering substances. Biochemic. J. 26, 2046–2055 (1932).
Davison, D. C.: The distribution of formic and alcohol dehydrogenase in the higher plants with particular reference to their variation in the pea during its life cycle. Proc. Linnean Soc. N. S. Wales 74, 26–36 (1949a).
The importance of formic dehydrogenase in the oxidative mechanisms of Pisum sativum. Proc. Linnean. Soc. N. S. Wales 74, 37–56 (1949b).
Studies on plant formic dehydrogenase. Biochemic. J. 49, 520–526 (1951).
Dawson, C. R.: The copper protein: ascorbic acid oxidase. In: Copper metabolism, pp. 18–47, Symposium McCollum-Pratt Institute, ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1950.
Day. R., and J. Franklin: Plant carbonic anhydrase. Science (Lancaster, Pa.) 104, 363–365 (1946).
Dickeman, S. R., and A. A. Cloutier: Activation and stabilisation of aconitase by ferrous ions. Arch. of Biochem. 25, 229–231 (1950).
Dixon, M.: Multienzyme systems. Cambridge: University Press 1949.
Dubnoff, J. W., and E. Bartron: The effect of B12 on enzyme activity in E. coli mutant 113–3. Arch. of Biochem. a. Biophysics 61, 99–110 (1956).
Ducet, G., and E. J. Hewitt: Relation of molybdenum status and nitrogen supply to respiration in cauliflower leaves. Nature (Lond.) 173, 1141–1142 (1954).
Ducet, G., et A. J. Rosenberg: Activité respiratoire chez les végétaux supérieurs. II. Activités cytochrome oxydasique et polyphenol-oxydasique chez quelques végétaux supérieurs. Bull. Soc. Chim. biol. Paris 33, 321–336 (1951).
Dunn, F. J., and C. R. Dawson: On the nature of ascorbic acid oxidase. J. of Biol. Chem. 189, 485–497 (1951).
Eichel, B., W. W. Wainio, P. Pierson and S. J. Cooperstein: A partial separation and characterisation of cytochrome oxidase and cytochrome b. J. of Biol. Chem. 183, 89–103 (1950).
Elliott, W. H.: Studies on the enzymic synthesis of glutamine. Biochemic. J. 49, 106–112 (1951).
Isolation of glutamine synthetase and glutamotransferase from green peas. J. of Biol. Chem. 201, 661–672 (1953).
Elvehjem, C. A.: The role of iron and copper in the growth and metabolism of yeast. J. of Biol. Chem. 90, 111–132 (1931).
Ephrussi, B., et P. P. Slonimski: La synthese adaptive des cytochromes chez la levure de boulangerie. Biochim. et Biophysica Acta 6, 256–267 (1950).
Euler, H. v., E. Adler, G. Gunther u. L. Elliott: Isocitronensäuredehydrase und Glutaminsäuresynthese in höheren Pflanzen und in Hefe. Enzymologia (Den Haag) 6, 337–341 (1939).
Euler, H. v., E. Adler, G. Gunther u. R. Vestin: Die Wirkungen von Cozymase, Adenylsäure und Cocarboxylase und ihre Beeinflussung durch Mn. Hoppe-Seylers Z. 247, 127–134 (1937).
Evans, H. J.: Diphosphopyridine nucleotide—nitrate reductase from soya bean root nodules. Plant Physiol. 29, 298–300 (1954).
Evans, H. J., and A. Nason: Pyridine nucleotide — nitrate reductase from extracts of higher plants. Plant Physiol. 28, 233–254 (1953).
Evans, H. J., E. R. Purvis and F. E. Bear: Molybdenum nutrition of alfalfa. Plant Physiol. 25, 555–566 (1950).
Finkle, B. J., and D. Appleman: The effect of magnesium concentration on chlorophyll and catalase development in Chlorella. Plant Physiol. 28, 652–663 (1953).
Fleischer, W. E.: The relation between chlorophyll content and rate of photosynthesis. J. Gen. Physiol. 18, 573–595 (1935).
Foster, J. W., and F. W. Denison: Role of zinc in metabolism. Nature (Lond.) 166, 833–834 (1950).
Galston, A. W., and R. S. Baker: Studies on the physiology of light action. II. The photodynamic action of riboflavin. Amer. J. Bot. 36, 773–780 (1949).
Studies on the physiology of light action. III. Light activation of a flavoprotein enzyme by reversal of the naturally occurring inhibition. Amer. J. Bot. 38, 190–195 (1951).
Galston, A. W., J. Bonner and R. S. Baker: Flavoprotein and peroxidase as constituents of the indole-acetic acid oxidase of peas. Amer. J. Bot. 37, 677–678 (1950).
Flavoprotein and peroxidase as components of the indole-acetic acid oxidase system of peas. Arch. of Biochem. a. Biophysics 42, 456–469 (1953).
Galston, A. W., R. K. Bonnichsen and D. I. Arnon: The preparation of highly purified spinach leaf catalase. Acta Chim. Scand. 5, 781–790 (1951).
Galston, A. W., and L. Y. Dalberg: The adaptive function and physiological significance of indole-acetic acid oxidase. Amer. J. Bot. 41, 373–380 (1954).
Gauch, H. G., and W. M. Dugger jr.: The role of boron in the translocation of sucrose. Plant. Physiol. 28, 457–466 (1953).
George, P.: The nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. Biochemic. J. 54, 267–276 (1953).
Gilbert, J. B., M. C. Otey and V. E. Price: The enzymatic suscepti-bility of the red cobalt complexes of several dipeptides. J. of Biol. Chem. 190, 377–389 (1951).
Glenn, J. L., and F. L. Crane: Studies on metalloflavoproteins. V. The action of silico-molybdate in the reduction of cytochrome c by aldehyde oxidase. Biochim. et Biophysica Acta 22, 111–115 (1956).
Goddard, D. R.: Cytochrome c and cytochrome oxidase from wheat germ. Amer. J. Bot. 31, 270–276 (1944).
Goddard, D. R., and C. Holden: Cytochrome oxidase in the potato tuber. Arch. of Biochem. 27, 41–47 (1950).
Goddard, D. R., and B. J. D. Meuse: Respiration of higher plants. Annual. Rev. Plant Physiol. 1, 207–232 (1950).
Gortner, W. A., and M. Kent: Indole-acetic acid oxidase and an inhibitor in pineapple. J. of Biol. Chem. 204, 593–603 (1953).
Green, D. E., R. E. Basford and B. Mackler: The role of iron and copper in terminal electron transport, pp. 628–649 in Symposium on Inorganic Nitrogen Metabolism, ed. by W. E. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press. 1956.
Green, D. E., and H. Beinert: Xanthine oxidase, a molybdoflavoprotein. Biochim. et Biophysica Acta 11, 599–600 (1953).
Green, D. E., O. Herbert and V. Subrahmanyam: “Carboxylase”. J. of Biol. Chem. 138, 327–339 (1941).
Green, D. E., and D. Richter: Adrenaline and adrenochrome. Biochemic. J. 31, 596–616 (1937).
Grimm, P. W., and P. J.Allen: Promotion by zinc of the formation of cytochromes in Ustilago sphaerogena. Plant Physiol. 29, 369–377 (1954).
Haas, E., C. J. Harrer and T. R. Hogness: Cytochrome reductase. II. Improved method of isolation, inhibition and inactivation. J. of Biol. Chem. 143, 341–349 (1942).
Haas, E., B. L. Horecker and T. R. Hogness: Soluble cytochrome c oxidase. J. of Biol. Chem. 130, 427–428 (1939).
The enzymatic reduction of cytochrome c. J. of Biol. Chem. 136, 747–774 (1940).
Happold, F. C., and A. Struyvenberg: The activation of trypto-phanase apoenzyme by potassium, ammonium and rubidium ions. Biochemic. J. 58, 379–382 (1954).
Harrison, K.: Activation of fumaric hydrogenase by ferrous iron. Nature (Lond.) 172, 509 (1953).
Hartman, W. J., and G. Kalnitsky: The competitive effects of metal ions on citrate oxidation. Arch. of Biochem. 26, 6–14 (1950).
Hartree, E. F.: Haematin compounds, pp. 197–245 in Vol. 4 of “Modem methods of plant analysis”, ed. by K. Paech and M. V. Tracey. Heidelberg: Springer 1955.
Haskins, F. A., A. Tissières, H. K. Mitchell and M. B. Mitchell: Cytochrome and the succinic acid oxidase systems of poky strains of Neurospora. J. of Biol. Chem. 200, 819–826 (1953).
Healy, W. B., Cheng, Sze-chuch and W. D. Mc Elroy: Metal toxicity and iron deficiency effects on enzymes in Neurospora. Arch. of Biochem. a. Biophysics 54, 206–214 (1955).
Hellerman, L.: Reversible inactivations of certain hydrolytic enzymes. Physiologic. Rev. 17, 454–484 (1937).
Hellerman, L., and C. C. Stock: Activation of enzymes. IV. The specificity of arginase and the non-enzymatic hydrolysis of guanidino compounds, activating metal ions and liver arginase. J. of Biol. Chem. 125, 771–793 (1938).
Herbert, D.: Oxalacetic decarboxylase. Biochemic. J. 47, Proc. (i) (1950).
Hers, H. G.: Rôle du magnésium et du potassium dans la reaction fructokinasique. Biochim. et Biophysica Acta 8, 424–430 (1952).
Hewitt, E. J.: The role of the mineral elements in plant nutrition. Annual Rev. Plant Physiol. 2, 25–52 (1951).
The importance of molybdenum in the nutrition of horticultural plants. Report of the 13th Internat. Horticultural Congr. London I, pp. 375–385, 1952. Royal Horticultural Soc. London 1953.
Metal interrelationships in plant nutrition. 1. Effects of some metal toxicities on sugar beet, tomato, oat, potato and marrowstem kale grown in sand culture. J. of Exper. Bot. 4, 59–64 (1953).
Metal interrelationships in plant nutrition. 2. The relation of metal toxicity, molybdenum and nitrogen source to chlorophyll and magnesium content of beet in sand culture. J. of Exper. Bot. 5, 110–118 (1954a).
Modem methods of determining the mineral nutrient requirement of plants with special reference to the micronutrient elements. Rapport générale Section 11a 8th Internat. Botanical Congr., Paris (1954b).
Hewitt, E. J., and S. C. Agarwala: Reduction of triphenyltetrazolium chloride by plant tissues and its relation to molybdenum status. Nature (Lond.) 169, 545–546 (1952).
Hewitt, E. J., S. C. Agarwala and E. W. Jones: Effect of molybdenum status on the ascorbic acid content of plants in sand culture. Nature (Lond.) 166, 1119–1120 (1950).
Hewitt, E. J., E. G. Fisher and M. I. Candela: Factors affecting the activity of nitrate reductase in cauliflower plants. Long Ashton Res. St. Ann. Rep. 1955, 202–210.
Hewitt, E. J., and D. G. Hallas: The use of Aspergillus niger (van Tiegh). M strain as a test organism in the study of molybdenum as a plant nutrient. Plant a. Soil 3, 366–408 (1951).
Hewitt, E. J., and E. W. Jones: The production of molybdenum deficiency in plants in sand culture with special reference to tomato and Brassica crops. J. Pomol. a. Horticult. Sci. 23, 254–262 (1947).
Hewitt, E. J., E. W. Jones and A. H. Williams: Relation of molybdenum and manganese to the free amino acid content of the cauliflower. Nature (Lond.) 163, 681–682 (1949).
Hewitt, E. J., and C. C. Mc Cready: Relation of nitrogen supply to the molybdenum requirement of tomato plants grown in sand culture. Nature (Lond.) 174, 186 (1954).
Hill, R.: Oxido-reductions in chloroplasts. Adv. Enzymol 12, 1–39 (1951).
Hill, R., and E. F. Hartree: Hematin compounds in plants. Annual Rev. Plant Physiol. 4, 115–150 (1953).
Hill, R., and R. Scarisbrick: The Haematin compounds of leaves. New Phytologist 50, 98–111 (1951).
Hickey, R. J.: The inactivation of iron by 2′,2′,-bipyridyl and its effect on riboflavin synthesis by Clostridium acetobutylicum. Arch. of Biochem. 8, 439–447 (1945).
Holm-Hansen, O., G. C. Gerloff and F. Skoog: Cobalt as an essential element for blue-green algae. Physiol. Plantarum (Copenh.) 7, 665–675 (1954).
Honda, S. I.: Succinoxidase and cytochrome oxidase in barley roots. Plant Physiol. 30, 402–410 (1955).
Humphries, T. E.: Studies on an enzyme system from wheat germ catalysing the aerobic oxidation of reduced triphosphopyridine nucleotide. Plant Physiol. 30, 46–54 (1955).
ichioka, P. S., and D. I. Arnon: Molybdenum in relation to nitrogen metabolism. II. Assimilation of ammonium and urea without molybdenum by Scenedesmus. Physiol. Plantarum (Copenh.) 8, 552–560 (1955).
James, W. O.: The terminal oxidase in the respiration of the embryo and young roots in barley. Proc. Roy. Soc. Lond., Ser. B 141, 289–299 (1953).
James, W. O., and D. Boulter: Further studies of the terminal oxidases in the embryos and young roots of barley. New Phytologist 54, 1–12 (1955).
James, W. O., and J. M. Cragg: The ascorbic acid system as an agent in barley respiration. New Phytologist 42, 28–44 (1943).
James, W. O., E. A. H. Roberts, H. Beevers and P. C. De Kock: The secondary oxidation of amino acids by the catechol oxidase of Belladonna. Biochemic. J. 43, 626–636 (1948).
Jensen, H. L.: The influence of molybdenum, calcium and agar on nitrogen fixation by Azotobacter indicum. Proc. Linnean Soc. N. S. Wales 72, 299–310 (1947).
Jensen, H. L., and R. L. Betty: Nitrogen fixation by leguminous plants. III. The importance of molybdenum in symbiotic nitrogen fixation. Proc. Linnean Soc. N. S. Wales 68, 1–8 (1943).
Jensen, H. L., and D. Spencer: The influence of molybdenum and vanadium on nitrogen fixation by Clostridium butyricum and related organisms. Proc. Linnean Soc. N. S. Wales 72, 73–86 (1947).
Johnson,M. J.: Isolation and properties of a pure yeast polypeptidase. J. of Biol. Chem. 137, 575–586 (1941).
Johnson, M. J., and J. Berger: The enzymatie properties of peptidases. Adv. Enzymol. 2, 69–92 (1942).
Johnson, S. S., and S. S. Silva: The oxidation of L. ascorbic acid by plant enzymes. Biochemic. J. 31, 438–453 (1936).
Jones, L. H., L. B. Shepardson and C. A. Peters: The function of manganese in the assimilation of nitrates. Plant Physiol. 24, 300–306 (1949).
Joselow, M., and C. R. Dawson: The copper of ascorbic acid oxidase. Exchange studies with radioactive copper. J. of Biol. Chem. 191, 11–20 (1951).
Kachmar, J. F., and P. D. Boyer: Kinetic analysis of enzyme reactions. II. The potassium activation and cation inhibition of pyruvic phosphoferase. J. of Biol. Chem. 200, 669–682 (1952).
Kalckar, H. M.: Adenyl pyrophosphatase and myokinase. J. of Biol. Chem. 153, 355–367 (1944).
Kalnitsky, G., and C. H. Werkman: Enzymatic decarboxylation of oxaloacetate and carboxylation of pyruvate. Arch. of Biochem. 4, 25–40 (1943b).
Kalyanasundaram, R., and L. Saraswathi-Devi: Zinc in the metabolism of Fusarium vasinfectum. Atk. Nature (Lond.) 175, 945 (1955).
Kamen, M. D.: Symposium on electron transport in the metabolism of microorganisms. Part 2. Bacterial heme proteins. Bacter. Rev. 19, 250–262 (1955).
Kaplan, N. O.: Symposium on electron transport in the metabolism of microorganisms. Part 1. Mechanisms of electron transport in pyridine nucleotide and flavin systems. Bacter. Rev. 19, 235–250 (1955).
Kearney, E. B., and S. Englard: The enzymatic phosphorylation of riboflavin. J. of Biol. Chem. 193, 821–834 (1951).
Keilin, D.: Cytochrome and respiratory enzymes. Proc. Roy. Soc. Lond., Ser. B 104, 206–252 (1929).
Cytochrome and intracellular oxidase. Proc. Roy. Soc. Lond. 106, 418–444 (1930).
Haemoglobin in fungi. Occurrence of haemoglobin in yeast and the supposed stabilisation of the oxygenated cytochrome oxidase. Nature (Lond.) 172, 390–393 (1953).
Keilin, D., and E. F. Hartree: Coupled oxidation of alcohol. Proc. Roy. Soc. Lond., Ser. B 119, 141–159 (1936).
Cytochrome oxidase. Proc. Roy. Soc. Lond., Ser. B 125, 171–186 (1938).
Cytochrome and cytochrome oxidase. Proc. Roy. Soc. Lond., Ser. B 127, 167–191 (1939).
Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions. Biochemic. J. 60, 310–325 (1955).
Keilin, D., and T. Mann: On the haematin compound of peroxidase. Proc. Roy. Soc. Lond., Ser. B 122, 119–133 (1937).
Polyphenol-oxidase: purification, nature and properties. Proc. Roy. Soc. Lond., Ser. B 125, 187–204 (1938).
Laccase, a blue copper protein oxidase from the latex of Rhus succadanea. Nature (Lond.) 143, 23–24 (1939).
Some properties of laccase from the latex of lacquer trees. Nature (Lond.) 145, 304 (1940).
Keilin, D., and J. D. Smith: Haemoglobin and nitrogen fixation in the root nodules of leguminous plants. Nature (Lond.) 159, 692–694 (1947).
Keilin, D., and A. Tissières: Haemoglobin in moulds: Neurospora crassa and Penicillium notatum. Nature (Lond.) 172, 393–394 (1953).
Keilin, D., and Y. L. Wang: Haemoglobin in the root nodules of leguminous plants. Nature (Lond.) 155, 227–229 (1945).
Kenten, R. H.: The oxidation of indolyl-3-acetic acid by Waxpod bean root sap and peroxidase systems. Biochemic. J. 59, 110–121 (1955).
Kenten, R. H., and P. J. G. Mann: The oxidation of manganese by plant extracts in the presence of hydrogen peroxide. Biochemic. J. 45, 255–263 (1949).
The oxidation of manganese by peroxidase systems. Biochemic. J. 46, 67–73 (1950).
The action of peroxidase systems on ferrocyanide, molybdate, tungstate and vanadate. Biochemic. J. 50, 29–34 (1951).
The oxidation of manganese by enzyme systems. Biochemic. J. 52, 125–130 (1952).
The oxidation of certain dicarboxylic acids by peroxidase systems in presence of manganese. Biochemic. J. 53, 498–505 (1953).
Kern, M., and E. Racker: Activation of a DPNH oxidase by an oxidation product of ascorbic. acid. Arch. of Biochem. a. Biophysics 48, 235–236 (1955).
Kertesz, D.: Tyrosinase and polyphenoloxidase. The role of metallic ions in melanogenesis. Biochim. et Biophysica Acta 9, 170–179 (1952).
Kertesz, Z. I.: The pectic substances. New York: Interscience 1951.
Kielley, R. K.: Purification of liver xanthine oxidase. J. of Biol. Chem. 216, 405–412 (1955).
Klein, R. M.: The relation of gas exchange and tyrosinase activity of tomato tissues to the level of boron nutrition of the plants. Arch. of Biochem. 30, 207–214 (1951).
Klotz, I. M.: Thermodynamic and molecular properties of some metal-protein complexes, pp. 257–285 in: The Mechanism of Enzyme Action. Symposium. McCollum-Pratt Institute, ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1954.
Klotz, I. M., and W. C. L. Ming: Mediation by metals of the binding of small molecules by proteins. J. Amer. Chem. Soc. 76, 805–814 (1954).
Kornberg, A.: Reversible enzymatic synthesis of diphosphopyridine nucleotide and inorganic pyrophosphate. J. of Biol. Chem. 182, 779–793 (1950a).
Enzymatic synthesis of triphosphopyridine nucleotide. J. of Biol. Chem. 182, 805–813 (1950b).
Kornberg, A., I. Lieberman and E. S. Simms: Enzymatic synthesis of purine nucleotides. J. of Biol. Chem. 215, 417–427 (1955).
Kornberg, A., S. Ochoa and A. H. Mehler: Spectrophotometric studies on the decarboxylation of α-keto acids. J. of Biol. Chem. 174, 159–172 (1948).
Kornberg, A., and W. E. Pricer jr.: Di- and tri-phosphopyridine nucleotide isocitric dehydrogenases in yeast. J. of Biol. Chem. 189, 123–136 (1951).
Korkes, S., J. R. Stern, I. C. Gunsalus and S. Ochoa: Enzymic synthesis of citrate from pyruvate and oxaloacetate. Nature (Lond.) 166, 439–440 (1950).
Krampitz, L. O., and C. H. Werkmann: The enzymic decarboxylation of oxaloacetate. Biochemic. J. 35, 595–602 (1941).
Krebs, H. A.: The effect of inorganic salts on the decomposition of oxaloacetic acid. Biochemic. J. 36, 303–305 (1942).
Krishnan, P. S.: Studies on apyrase. II. Some properties of potato apyrase. Arch. of Biochem. 20, 272–283 (1949).
Kubo, H.: Acta phytochim. (Tokyo) 11, 195 (1939). Cited by Keilin and Wang 1945.
Kubowitz, F.: Über die chemische Zusammensetzung der Kartoffeloxydase. Biochem. Z. 292, 221–229 (1937).
Spaltung und Resynthese der Polyphenoloxydase und des Hämocyanins. Biochem. Z. 299, 32–57 (1938).
Kunitz, M.: Crystalline inorganic pyrophosphatase isolated from baker’s yeast. J. Gen. Physiol. 35, 423–450 (1952).
Lajtha, A., P. Mela and H. Waelsh: Manganese dependent glutamyl transferase. J. of Biol. Chem. 205, 553–564 (1953).
Lampit, L. H., and D. H. F. Clayson: The nature of ascorbic acid oxidase. I. A critique of the copper-protein theory. Biochemic. J. 39, Proc. XV (1945).
Lardy, H. A.: The influence of inorganic ions on phosphorylation reactions I, pp. 477–499 in: Phosphorus metabolism. Symposium. McCollum-Pratt Institute Ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press. 1951.
Lardy, H. A., and J. A. Ziegler: The enzymatic synthesis of phosphopyruvate from pyruvate. J. of Biol. Chem. 159, 343–351 (1945).
Lehninger, A. L.: Role of metal ions in enzyme systems. Physiologic. Rev. 30, 393–429 (1950).
Lenhoff, H. M., and N. O. Kaplan: A cytochrome peroxidase from Pseudomonas fluorescens. Nature (Lond.) 172, 730–731 (1953).
A cytochrome peroxidase from Pseudomonas fluorescens. J. of Biol. Chem. 1956.
Lenhoff, H. M., D. J. D. Nicholas and N. O. Kaplan: Effects of oxygen, iron and molybdenum on alternative routes of electron transfer in Pseudomonas fluorescens. J. of Biol. Chem. 220, 983–995 (1956).
Levy, H., and A. L. Schade: Studies in the respiration of the white potato. II. Terminal oxidase systems of the potato tuber respiration. Arch. of Biochem. 19, 273–286 (1948).
Lieberman, I., A. Kornberg and E. S. Simms: Enzymatic synthesis of pyrimidine nucleotides. Orotidine 5 phosphate and Uridine 5 phosphate. J. of Biol. Chem. 215, 403–415 (1955a).
Enzymatic Synthesis of nucleotide diphosphates and triphosphates. J. of Biol. Chem. 215, 429–440 (1955b).
Loneragen, J., and D. I. Arnon: Molybdenum in the growth and metabolism of Chlorella. Nature (Lond.) 174, 459 (1954).
Lotspeich, W. D., and R. A. Peters: The action of sulphydryl inhibitors upon isocitric dehydrogenase with especial reference to the behaviour of some trivalent arsenicals. Biochemic. J. 49, 704–709 (1951).
Lovett-Janison, P. L., and J. M. Nelson: Ascorbic acid oxidase from summer crook-neck squash (C. pepo condensa). J. Amer. Chem. Soc. 62, 1409–1412 (1946).
Lulla, B. S.: Studies in bacterial amylase. III. Influence of the concentration of the cultural nutrients on the formation of bacterial amylase. Biochim. et Biophysica Acta 7, 244–250 (1951).
Lundegårdh, H.: Spectroscopic evidence of the participation of the cytochrome—cytochrome oxidase system in the active transport of salts. Nature (Lond.) 167, 71 (1951).
Properties of the cytochrome system of living wheat roots. Nature (Lond.) 169, 1088–1091 (1952).
Controlling effect of salts on the activity of the cytochrome oxidase. Nature (Lond.) 171, 477–478 (1953).
On the oxidation of cytochrome f by light. Physiol. Plantarum (Copenh.) 7, 375–382 (1954).
Mackler, B., H. R. Mahler and D. E. Green: Studies on metallo-flavoproteins. I. Xanthine oxidase, a molybdo-flavo protein. J. of Biol. Chem. 210, 149–164 (1954).
Mac Vicar, R., and R. H. Burris: The relation of boron to certain plant oxidases. Arch. of Biochem. 17, 31–39 (1948).
Mahler, H. R.: Butyryl CoA-dehydrogenase, a cupro-flavoprotein. J. Amer. Chem. Soc. 75, 3288–3289 (1953).
Studies on the fatty acid oxidising system of animal tissues. IV. The prosthetic group of butyryl Co enzyme A dehydrogenase. J. of Biol. Chem. 206, 13–26 (1954).
Nature and functions of metallo-flavoproteins. Adv. Enzymol. 17, 233–291 (1956).
Mahler, H. R., and D. G. Elowe: DPNH cytochrome reductase, a ferro-flavoprotein. J. Amer. Chem. Soc. 75, 5769–5770 (1953).
Studies on metallo-flavoproteins. II. The role of iron in diphosphopyridine nucleotide cytochrome c reductase. J. of Biol. Chem. 210, 165–179 (1954).
Mahler, H. R., and J. L. Glenn: General significance of metallo-flavoproteins in electron transport, pp. 575–597 in Symposium on “Inorganic nitrogen nutrition,” ed. by W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press. 1956.
Mahler, H. R., B. Mackler, D. E. Green and R. M. Bock: Studies on metalloflavoproteins. III. Aldehyde oxidase, a molybdoflavoprotem. J. of Biol. Chem. 210, 465–480 (1954).
Mallette, M. F.: The nature of the copper enzymes involved in tyrosine oxidation, pp. 48–75 in: Copper metabolism. Symposium. McCollum-Pratt Institute, Ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1950.
Mallette, M. F., and C. R. Dawson: On the nature of highly purified mushroom tyrosinase preparations. Arch. of Biochem. 23, 29–44 (1949).
Malmstrom, B. G.: Interaction of manganous ions with enolase. Nature (Lond.) 171, 392–393 (1953a).
The interaction of enolase with its activating metals. Arch. of Biochem. a. Biophysics 46, 345–363 (1953b).
Mapson, L. W.: Function of ascorbic acid in plants. Vitamins a. Hormones 11, 1–28 (1953).
Mapson, L. W., and D. R. Goddard: The reduction of glutathione by plant tissues. Biochemic. J. 49, 592–601 (1951).
Mapson, L. W., F. A. Isherwood and Y. T. Chen: Biological synthesis of l-ascorbic acid: the conversion of l-galactono γ-lactone into l-ascorbic acid by plant mitochrondria. Biochemic. J. 56, 21–28 (1954).
Marsh, P. B., and D. R. Goddard: Respiration and fermentation in the carrot. Daucus carota. II. Fermentation and the Pasteur effect. Amer. J. Bot. 26, 767–772 (1939).
Martin, E. M., and R. K. Morton: Cytochrome b3 of microsomes from plant tissues. Nature (Lond.) 176, 113–114 (1955).
Maschmann, E.: Über Bakterienproteasen. XII. Zur Kenntnis der Dipeptidasen anaerober Bakterien. Biochem. Z. 302, 332–368 (1939).
Maskell, E. J., H. Evans and D. B. Murray: Report on cocoa research 1945–1951, pp. 53–64. Imp. Coll. Trop. Agr. St. Augustine, Trinidad 1953.
Mason, H. S.: Structure and functions of the phenolase complex. Nature (Lond.) 177, 79–81 (1956).
Massart, L., u. L. Vandendriessche: Aktivierung und Hemmung des Phosphatasen. Naturwiss. 28, 143 (1940).
Mathews, M. B.: The oxidation of reduced diphosphopyridine nucleotide in green peas. J. of Biol. Chem. 189, 695–704 (1951).
Mathews, M. B., and B. Vennesland: Enzymic oxidation of formic acid. J. of Biol. Chem. 186, 667–682 (1950).
Maxwell, R. E.: Cytochrome oxidase in corn embryos. Plant Physiol. 25, 521–524 (1950).
Mc Elroy, W. D.: The role of trace elements in enzyme systems, pp. 262–286 in Symposium on Nutrition, Ed. R. M. Herriott. Baltimore: Johns Hopkins Press 1953.
Mc Elroy, W. D., and A. Nason: Mechanism of action of micronutrient elements in enzyme systems. Annual Rev. Plant Physiol. 5, 1–30 (1954).
Mc Nair Scott, D. B. and S. S. Cohen: The oxidative pathway of carbohydrate metabolism in Escherichia coli. Biochemic. J. 55, 23–33 (1953).
Mee, S.: A study of carboxylase in soybean seeds. Arch. of Biochem. 22, 139–148 (1949).
Merry, J., and D. R. Goddard: A respiratory study of barley grains and seedlings. Proc. Rochester Acad. Sci. 8, 28–44 (1941).
Meyerhof, O.: The origin of the reaction of Harden and Young in cell free alcoholic fermentation. J. of Biol. Chem. 157, 105–119 (1945).
Michaelis, L.: Oxidation-reduction systems of biological importance. VI. The mechanism of the catalytic effect of iron on the oxidation of cysteine. J. of Biol. Chem. 84, 777–787 (1929).
Miller, G., and H. J. Evans: The influence of salts on pyruvate kinase from tissues of higher plants. Plant Physiol. 32, 346–354 (1957).
Miyaji, T., and J. P. Greenstein: Cation activation of desoxyribonuclease. Arch. of Biochem. a. Biophysics 32, 414–423 (1951).
Morrison, J. F.: The purification of aconitase. Biochemic. J. 56, 99–105 (1954).
Moyle, J., and M. Dixon: The identity of TPN linked isocitric dehydrogenase and oxalosuccinic decarboxylase. Biochim. et Biophysica Acta 16, 434–435 (1955).
Mulder, E. G.: Importance of molybdenum in the nitrogen metabolism of micro-organisms and higher plants. Plant a. Soil, 1, 94–119 (1948).
Mineral nutrition of plants. Annual Rev. Plant Physiol. 1, 1–24 (1950).
Molybdenum in relation to growth of higher plants and micro-organisms. Plant a. Soil, 5, 368–415 (1954).
Muntz, J. A.: The role of potassium and ammonium ions in alcoholic fermentation. J. of Biol. Chem. 171, 653–655 (1947).
Naganna, B., A. Raman, B. Venugopal and C. E. Sripathi: Potato pyrophosphatases. Biochemic. J. 60, 215–223 (1955).
Naganna, B., B. Venugopal and C. E. Sripathi: Occurrence of alkaline pyrophosphatase in vegetable tissues. Biochemic. J. 60, 224–225 (1955).
Najjar, V. A.: The role of metal ions in enzyme systems, pp. 500–520 in McCollum-Pratt Symposium on Phosphorous metabolism, Vol. I, Ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1951.
Nason, A.: Effect of zinc deficiency on the synthesis of tryptophane by Neurospora extracts. Science (Lancaster, Pa.) 112, 111–112 (1950).
Metabolism of micronutrient elements in higher plants. II. Effect of copper deficiency on the isocitric enzyme in tomato leaves. J. of Biol. Chem. 198, 643–653 (1952).
Nason, A., R. G. Abraham and B. C. Averbach: The enzymic reduction of nitrite to ammonia by reduced pyridine nucleotides. Biochim. et Biophysica Acta 15, 160–161 (1954).
Nason, A., and H. Evans: Triphosphopyridine nucleotide-nitrate reductase in Neurospora. J. of Biol. Chem. 202, 655–673 (1953).
Nason, A., N. O. Kaplan and S. P. Colowick: Changes in enzymatic constitution in zinc deficient Neurospora. J. of Biol. Chem. 188, 397–406 (1951).
Nason, A., N. O. Kaplan and H. A. Oldewurtel: Futher studies of nutrient conditions affecting enzymatic constitution in Neurospora. J. of Biol. Chem. 201, 435–444 (1953).
Nason, A., H. A. Oldewurtel and L. M. Propst: Role of micro-nutrient elements in the metabolism of higher plants. I. Changes in oxidative enzyme constitution of tomato leaves deficient in micronutrient elements. Arch. of Biochem. a. Biophysics 38, 1–13 (1952).
Nason, A., W. D. Wosilait and A. J. Terrell: The enzymatic oxidation of reduced pyridine nucleotides by an oxidation product of ascorbic acid. Arch. of Biochem. a. Biophysics 48, 233–235 (1954).
Neish, A. C.: Studies on chloroplasts. II. Their chemical composition and the distribution of certain metabolites between the chloroplasts and the remainder of the leaf. Biochemic. J. 33, 300–308 (1939).
Nelson, J. M.: Phenol oxidases and plant respiration, pp. 76–88 in: Copper Metabolism. Symposium of the McCollum-Pratt Institute, Ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1950.
Nelson, J. M., and C. R. Dawson: Tyrosinase. Adv. Enzymol. 4, 99–152 (1944).
Newcomb, E. H.: Effect of auxin on ascorbic oxidase activity in tobacco pith cells. Proc. Soc. Exper. Biol. a. Med. 76, 504–509 (1951).
The use of cultured tissue in a study of the metabolism controlling cell enlargement. Année Biol. 31, 195–214 (1955).
Nicholas, D. J. D.: The use of fungi for determining trace metals in biological materials. Analyst (Lond.) 77, 629–642 (1952).
Nicholas, D. J. D., and A. Nason: Molybdenum and nitrate reductase. II. Molybdenum as a constituent of nitrate reductase. J. Biol. Chem. 207, 353–360 (1954a).
Molybdenum as an electron carrier in nitrate reductase action. Arch. of Biochem. a. Biophysics 51, 311–312 (1954b).
Mechanisms of action of nitrate reductase from Neurospora. J. of Biol. Chem. 211, 183–197 (1954c).
Role of molybdenum as a constituent of nitrate reductase from soya bean leaves. Plant Physiol. 30, 135–138 (1955a).
Diphosphopyridine nucleotide reductase from Escherichia coli. J. Bacter. 69, 580–583 (1955b).
Nicholas, D. J. D., A. Nason and W. D. Mc Elroy: Effect of molybdenum deficiency on nitrate reductase in cell free extracts of Neurospora and Aspergillus. Nature (Lond.) 172, 34–35 (1953).
Molybdenum and nitrate reductase. I. Effect of molybdenum deficiency on the Neurospora enzyme. J. of Biol. Chem. 207, 341–351 (1954).
Nicholas, D. J. D., and H. M. Stevens: The role of molybdenum in oxidation-reduction processes in Neurospora and Azotobacter. In: A symposium on inorganic nitrogen metabolism, pp. 178–183, Ed. by W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1956.
Nickerson, W. J.: Enzymatic control of cell division in microorganisms. Nature (Lond.) 162, 241–245 (1948).
Nickerson, W. J., and N. J. W. van Rij: The effect of sulphydryl compounds, penicillin and cobalt on the cell division mechanism of yeast. Biochim. et Biophysica Acta 3, 461–475 (1949).
Nickerson, W. J., and K. Zerahn: Accumulation of radioactive cobalt by dividing yeast cells. Biochim. et Biophysica Acta 3, 476–483 (1949).
Ochoa, S.: Isocitric dehydrogenase and carbon dioxide fixation. J. of Biol. Chem. 159, 243–244 (1945).
Biosynthesis of tricarboxylic acids by carbon dioxide fixation. III. Enzymatic mechanisms. J. of Biol. Chem. 174, 133–157 (1948).
Ochoa, S., A. H. Mehler and A. Kornberg: Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I. Isolation and properties of an enzyme from pigeon liver catalysing the reversible oxidative decarboxylation of l-mahc acid. J. of Biol. Chem. 174, 979–1000 (1948).
Ochoa, S., and E. Weisz-Tabori: Oxalosuccinic carboxylase. J. of Biol. Chem. 159, 245–246 (1945).
Packer, L., and W. Vishniac: The specificity of a diphosphopyridine nucleotide linked hydrogenase. Biochim. et Biophysica Acta 17, 153–154 (1953).
Paladini, A. C., R. Caputto, L. F. Leloir, R. E. Trucco and C. E. Cardini: The enzymatic synthesis of glucose 1–6 diphosphate. Arch. of Biochem 23, 55–66 (1949).
Pinsent, J.: Molybdenum and formic dehydrogenase of bacteria. J. Gen. Microbiol. 3, Proc. XII (1949).
The need for selenite and molybdate by members of the Coli-Aerogenes group of bacteria. Biochemic. J. 57, 10–16 (1954).
Pirson, A.: Functional aspects of mineral nutrition of green plants. Annual Rev. Plant Physiol. 6, 71–114 (1955).
Plaut, G. W. E., and H. A. Lardy: The oxalacetic decarboxylase of Azotobacter vinelandii. J. of Biol. Chem. 180, 13–27 (1949).
Possingham, J. V.: The effect of molybdenum on the organic and inorganic phosphorus of plants. Austral. J. Biol. Sci. 7, 221–224 (1954).
Powers, W. H., S. Lewis and C. R. Dawson: Preparation and properties of highly purified ascorbic acid oxidase. J. Gen. Physiol. 27, 167–180 (1944).
Pratt, R., and J. Dufrenoy: Cytochemical interpretation of the mechanism of penicillin action. Bacter. Rev. 12, 79–103 (1949).
Quinlan-Watson, T. A. F.: Aldolase activity in zinc deficient plants. Nature (Lond.) 167, 1033–1034 (1951).
The effect of zinc deficiency on the aldolase activity in the leaves of oats and clover. Biochemic. J. 53, 457–460 (1953).
Ramakrishnan, C. V., and S. M. Martin: Isocitric dehydrogenase in Aspergillus niger. Arch. of Biochem. a. Biophysics 55, 403–407 (1955).
Ramasarma, T., J. Ram and K. V. Giri: Phosphoglucomutase of green gram (Phaseolus radiatus). Arch. of Biochem. a. Biophysics 53, 167–173 (1954).
Reed, H. S.: Effects of zinc deficiency on phosphate metabolism of the tomato plant. Amer. J. Bot. 33, 778–784 (1946).
Reen, R. van: The influence of excessive dietary molybdenum on rat liver enzymes. Arch. of Biochem. a. Biophysics 53, 77–84 (1954).
Reinert, J., and P. R. White: The cultivation in vitro of tumor tissues and normal tissues of Pinus glauca. Physiol. Plantarum (Copenh.) 9, 177–189 (1956).
Renzo, E. C. de, P. G. Heytler and E. Kaleita: Further evidence that molybdenum is a co-factor of xanthine oxidase. Arch. of Biochem. a. Biophysics 49, 242–244 (1954).
Renzo, E. C. de, E. Kaleita, P. G. Heytler, J. J. Oleson, B. L. Hutchings and J. H. Williams: Identification of the xanthine oxidase factor as molybdenum. Arch. of Biochem. a. Biophysics 45, 247–253 (1953).
Richards, F. J., and E. Berner jr.: Physiological studies in plant nutrition. XVII. A general survey of the free amino acids of barley as affected by mineral nutrition with special reference to potassium supply. Ann. of Bot., N. S. 18, 15–33 (1954).
Richert, P. A., and W. W. Westerfeld: Isolation and identification of the xanthine oxidase factor as molybdenum. J. of Biol. Chem. 203, 915–923 (1953).
The relationship of iron to xanthine oxidase. J. of Biol. Chem. 209, 179–189 (1954).
Roach, W. A., and C. Barclay: Nickel and multiple trace elements in agricultural crops. Nature (Lond.) 157, 696–697 (1946).
Robinson, E. S., and J. M. Nelson: The tyrosine-tyrosinase reaction and aerobic plant respiration. Arch. of Biochem. 4, 111–117 (1944).
Rosen, W. G.: Plant growth inhibition by streptomycin and its prevention by manganese. Proc. Soc. Exper. Biol. a. Med. 85, 385–388 (1954).
Rosenberg, A. J., et G. Ducet: Activité cytochromoxydasique chez l’epinard. C. r. Acad. Sci. Paris 229, 391–393 (1949).
Rudkin, G. O., and J. M. Nelson: Chlorogenic acid and respiration of sweet potato tubers. J. Amer. Chem. Soc. 69, 1470–1475 (1947).
Sadasivan, V.: Biochemical studies on Penicillium chrysogenum. I. Phosphatase activity and the role of zinc in the production of penicillin. Arch. of Biochem. a. Biophysics 28, 100–110 (1950).
Nature of phosphatase activity. Nature (Lond.) 169, 418–419 (1952).
Saltmann, P.: Hexokinase in higher plants. J. of Biol. Chem. 200, 145–154 (1953).
Sato, R., and F. Egami: Nitrate reductase. III. Bull. Chem. Soc. Japan 22, 137–143 (1949). (Chem. Abstr. 1950 [44], 6454.)
Sato, R., and M. Niwa: Studies on nitrate reductase. VII. Reinvestigation on the identity of the enzyme with cytochrome b. Bull. Chem. Soc. Japan 25, 202–210 (1952).
Saz, A., and R. B. Shi: Manganese reversal of aureomycin inhibition of bacterial cell-free nitroreductase. J. Amer. Chem. Soc. 75, 4626–4627 (1953).
Schade, A. L., and H. Levy: Studies on the respiration of the white potato. III. Changes in the terminal oxidase pattern of potato tissue associated with time of suspension in water. Arch. of Biochem. 20, 211–219 (1949).
Schales, O., and R. M. Roux: Iron and dihydroxyphenyl-alanine as activators for leucylglycine dipeptidase from yeast. J. of Biol. Chem. 182, 569–576 (1950).
Schales, O., S. S. Schales and G. M. Schwarzenbach: Federat. Proc. 9, 223 (1950). Cited by Mc Elroy and Nason 1954.
Schrecker, A. W., and A. Kornberg: Reversible enzymatic synthesis of flavinadeninedinucleotide. J. of Biol. Chem. 182, 795–803 (1950).
Schultze, M. O.: The effect of deficiencies in copper and iron on the cytochrome oxidase of rat tissues. J. of Biol. Chem. 129, 729–737 (1939).
Seifter, E.: The occurrence of co-enzyme A in plants. Plant Physiol. 29, 403–406 (1954).
Seitz, I. F.: Role of potassium and ammonium ions in the transfer of phosphate to the adenylic system. Biokhimiya 14, 134–140 (1949).
Shorb, M. S.: Activity of vitamin B12 for the growth of Lactobacillus lactis. Science (Lancaster, Pa.) 107, 397–398 (1948).
Shug, A. L., P. W. Wilson, D. E. Green and M. R. Mahler: The role of molybdenum and flavin in hydrogenase. J. Amer. Chem. Soc. 76, 3355–3356 (1954).
Sibley, P. M., and I. G. Wood: The nature of carbonic anhydrase from plant sources. Austral. J. Sci. Res. B 4, 500–510 (1951).
Sideris, C. P., and H. Y. Young: Growth and chemical composition of Ananas comosus (L.) Merr. in solution cultures with different iron-manganese rations. Plant Physiol. 24, 416–440 (1949).
Singer, T. P., and E. B. Kearney: The non-enzymatic reduction of cytochrome c by pyridine nucleotides and its catalysis by various flavins. J. of Biol. Chem. 183, 409–429 (1950).
Solubilization, assay and purification of succinic dehydrogenase. Biochim. et Biophysica Acta 15, 151–153 (1954).
Slater, E. C.: A respiratory catalyst required for the reduction of cytochrome c by cytochrome b. Biochemic. J. 45, 14–30 (1949).
The components of the dihydro-cozymase system. Biochemic. J. 46, 484–499 (1950).
Smith, E. L., N. C. Davis, E. Adams and D. H. Spackman: The specificity and mode of action of two metal-peptidases, pp. 291–318 in: The mechanism of Enzyme Action. Symposium. McCollum-Pratt Institute, Ed. W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1954.
Smith, J. D.: The concentration and distribution of haemoglobin in the root nodules of leguminous plants. Biochemic. J. 44, 585–591 (1949a).
Haemoglobin and the oxygen uptake of leguminous root nodules. Biochemic. J. 44, 591–598 (1949b).
Snoke, J. C.: Isolation and properties of yeast glutathione synthetase. J. of Biol. Chem. 213, 813–824 (1955).
Speck, J. F.: The effect of cations on the decarboxylation of oxalacetic acid. J. of Biol. Chem. 178, 315–324 (1949).
Spencer, D.: The effect of molybdate on the activity of tomato acid phosphatases. Austral. J. Biol. Sci. 7, 151–160 (1954).
Spencer, D., and J. G. Wood: The role of molybdenum in nitrate reduction in higher plants. Austral. J. Biol. Sci. 7, 425–434 (1955).
Stadtman, E. R.: The purification and properties of phosphotransacetylase. J. of Biol. Chem. 196, 527–534 (1952).
Steinberg, R. A.: Effects of nitrogen compounds and trace elements on growth of Aspergillus niger. J. Agricult. Res. 59, 731–748 (1939).
Steinberger, R., and F. H. Westheimer: The metal ion-catalysed decarboxylation of dimethyl-oxaloacetic acid. J. Amer. Chem. Soc. 71, 4158–4159 (1949).
Metal ion-catalysed decarboxylation: a model for an enzyme system. J. Amer. Chem. Soc. 73, 429–435 (1951).
Stern, J. R., B. Shapiro and S. Ochoa: Synthesis and breakdown of citric acid with crystalline condensing enzyme. Nature (Lond.) 166, 403–404 (1950).
Stickland, L. H.: The activation of phosphoglucomutase by metal ions. Biochemic. J. 44, 190–197 (1949).
Stock, C. C., M. E. Perkins and L. J. Hellerman: Activation of enzymes. IV. The jackbean arginolytic enzyme. J. of Biol. Chem. 125, 753–769 (1938).
Stotz, E., A. M. Altschul and T. R. Hogness: The cytochrome c-cytochrome oxidase complex. J. of Biol. Chem. 124, 745–754 (1938).
Stotz, E., C. J. Harrer and C. G. King: A study of “ascorbic acid oxidase” in relation to copper. J. of Biol. Chem. 119, 511–522 (1937).
Stotz, E., G. J. Harrer, M. O. Schultze and C. G. King: The oxidation of ascorbic acid in the presence of guinea pig liver. J. of Biol. Chem. 122, 407–418 (1938).
Stotz, E., A. E. Sidwell jr. and T. R. Hogness: The role of the cytochromes in the action of “indophenol oxidase”. J. of Biol. Chem. 124, 733–744 (1938).
Stumpf, P. K.: Pyruvic oxidase of Proteus vulgaris. J. of Biol. Chem. 159, 529–544 (1945).
Carbohydrate metabolism in higher plants. I. Pea aldolase. J. of Biol. Chem. 176, 233–241 (1948).
Carbohydrate metabolism in higher plants. III. Breakdown of fructose diphosphate by pea extracts. J. of Biol. Chem. 182, 261–272 (1950).
Stumpf, P. K., and W. D. Loomis: Observations on a plant amide enzyme system requiring manganese and phosphate. Arch. of Biochem. 25, 451–453 (1950).
Stumpf, P. K., W. D. Loomis and C. Mitchelson: Amide metabolism in higher plants. I. Preparation and properties of a glutamyl transphorase from pumpkin seedling. Arch. of Biochem. 30, 126–137 (1951).
Sumner, J. B., and G. F. Somers: Chemistry and methods of enzymes, 3rd ed. New York: Academic Press 1953.
Swedin, B., and H. Theorell: Dioxymaleic acid oxidase action of peroxidases. Nature (Lond.) 145, 71–72 (1940).
Tang, Yu-Wei, and J. Bonner: The enzymatic inactivation of indolacetic I. Some characteristics of the enzyme contained in pea seedlings. Arch. of Biochem. 13, 11–25 (1947).
Taniguchi, S., R. Sato and F. Egami: The enzymatic mechanism of nitrate and nitrite metabolism in bacteria, pp. 87–108 in Symposium on “Inorganic nitrogen metabolism,” ed. by W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Univ. Press 1956.
Theorell, H.: Ark. Kemi, Mmeral. Geol. B 14, No 20, 1 (1940). Cited by Sumner and Somers 1953.
Theorell, H., u. B. Swedin: Mangan als Aktivator der Dioxymaleinsäureoxydase. Naturwiss. 27, 95 (1939).
Thimann, K. V., C. S. Yocum and D. P. Hackett: Terminal oxidases and growth in plant tissues. III. Terminal oxidation in potato tuber tissue. Arch. of Biochem. a. Biophysics 53, 239–257 (1954).
Thoai, N. V., J. Roche et M. Rogers: Inactivation et réactivation complètes de la Phosphomonoestérase alcaline et interchangibilité des metaux actifs. Biochim. et Biophysica Acta 1, 61–76 (1943).
Thoai, N. V., J. Roche et J. M. Verrier: Sur les complexes cobaltiques de l’arginase hépatique et de l’argine ou d’inhibiteurs concurrents de celle ci. C. r. Acad. Sci. Paris 236, 2008–2010 (1953).
Tissières, A.: Reconstruction of laccase from its protein and copper. Nature (Lond.) 162, 340–341 (1948).
Constitution and properties of laccase. Nature (Lond.) 163, 480 (1949).
Tissières, A., and H. K. Mitchell: Cytochromes and respiratory activities in some slow growing strains of Neurospora. J. of Biol. chem. 208, 241–249 (1954).
Tolmach, L. J.: Effects of triphosphopyridine nucleotide upon oxygen evolution and carbon dioxide fixation by illuminated chloroplasts. Nature (Lond.) 167, 946–948 (1951).
Totter, J. R., W. T. Burnett jr., R. A. Monroe, I. B. Whitney and C. L. Comar: Evidence that molybdenum is a non-dialysible component of xanthine oxidase. Science (Lancaster, Pa.) 118, 555 (1953).
Trucco, R. F., R. Caputto, L. F. Leloir and N. Mittelman: Galactokinase. Arch. of Biochem. 18, 137–146 (1948).
Tsui, Chen: The role of zinc in auxin synthesis in the tomato plant. Amer. J. Bot., 35, 172–178 (1948).
Utter, M. F., and C. F. Werkman: Effect of metal ions on the reactions of phosphopyruvate by Escherichia coli. J. of Biol. Chem. 146, 289–300 (1942).
Vallee, B. L., and F. L. Hoch: Yeast alcohol dehydrogenase, a zinc metallo-enzyme. J. Amer. Chem. Soc. 77, 821–822 (1955).
Vallee, B. L., F. L. Hoch, S. J. Adelstein and W. E. L. Waiker: Pyridine nucleotide-dependant metallo-dehydrogenases. J. Amer, Chem. Soc. 78, 5879–5883 (1956).
Veiga-Salles, J. B., I. Harary, R. F. Barfi and S. Ochoa: Enzymatic incorporation of carbon dioxide in oxaloacetate in pigeon liver. Nature (Lond.) 165, 675–676 (1950).
Veiga-Salles, J. B., and S. Ochoa: Biosynthesis of dicarboxyhc acids by carbon dioxide fixation. II. Further study of the properties of the malic enzyme of pigeon liver. J. of Biol. Chem. 187, 849–861 (1950).
Vennesland, B.: The β-carboxylases of plants. III. The distribution of oxaloacetic carboxylase in plant tissues. J. of Biol. Chem. 178, 591–597 (1949).
Vennesland, B., J. Ceithamel and M. C. Gollub: The fixation of carbon dioxide in a plant tricarboxylic acid system. J. of Biol. Chem. 171, 445–446 (1947).
Vennesland, B., E. A. Evans jr. and A. M. Francis: The action of metmyoglobin, oxygen and manganese on oxaloacetic acid. J. of Biol. Chem. 163, 573–574 (1946).
Vennesland, B., and R. Z. Felsher: Oxaloacetic and pyruvic carboxylases in some dicotyledonous plants. Arch. of Biochem. 11, 279–306 (1946).
Vennesland, B., M. C. Gollub and J. F. Speck: The carboxylases of plants. I. Some properties of oxaloacetic carboxylase and its quantitative assay. J. of Biol. Chem. 178, 301–314 (1949).
Virtanen, A.: The biology and chemistry of nitrogen fixation by legume bacteria. Biologic. Rev. 22, 239–269 (1947).
Vishniac, W., and S. Ochoa: Photochemical reduction of pyridine nucleotides by spinach grana and coupled carbon dioxide fixation. Nature (Lond.) 167, 768–769 (1951).
Phosphorylation coupled to photochemical reduction of pyridine nucleotides by chloroplast preparations. J. of Biol. Chem. 198, 501–506 (1952).
Wagenknecht, A. C., and R. H. Burris: Indoleacetic acid inactivating enzymes from bean roots and pea seedlings. Arch. of Biochem. 25, 30–53 (1950).
Wang, T. P.: Specific 5′-nucleotidase from a soil bacterium. J. Bacter. 68, 128 (1954).
Wang, T. P., and N. O. Kaplan: Kinases for the synthesis of co-enzyme A and triphosphopyridine nucleotide. J. of Biol. Chem. 206, 311–325 (1954).
Warburg, O., u. W. Christian: Isolierung und Kristallisation des Gärungsferments Enolase. Biochem. Z. 310, 384–421 (1942a).
Wirkungs-gruppe des Gärungsferments Zymohexase. Biochem. Z. 311, 209–210 (1942b).
Isolierung und Kristallisation des Gärungsferments Zymohexase. Biochem. Z. 314, 149–176 (1943).
Waring, W. S., and C. H. Werkmann: Iron deficiency in bacterial metabolism. Arch. of Biochem. 4, 75–87 (1944).
Waygood, E. R.: Physiological and biochemical studies in plant metabolism. II. Respiratory enzymes in wheat. Canad. J. Res. 28, 7–62 (1950).
Waygood, E. R., and K. A. Clendenning: Carbonic anhydrase in green plants. Canad. J. Res. C 28, 673–689 (1950).
Waygood, E. R., and C. A. Mac Lachlan: The effect of catalase, riboflavin and light on the oxidation of indoleacetic acid. Physiol. Plantarum (Copenh.) 9, 607–617 (1956).
Waygood, E. R., A. Oaks and G. A. Mac Lachlan: On the mechanism of indoleacetic acid oxidation by wheat leaves. Canad. J. Bot. 34, 54–59 (1956a).
The enzymatically catalysed oxidation of indoleacetic acid. Canad. J. Bot. 34, 905–926 (1956b).
Webb, M. M., H. M. Lenhofp and N. O. Kaplan: The function of inorganic iron in the reduction of cytochrome c. Biochim. et Biophysica Acta 14, 298–299 (1954).
Webster, G. C.: The occurrence of a cytochrome oxidase in the tissues of higher plants. Amer. J. Bot. 38, 379–445 (1952).
Peptide bond synthesis in higher plants. I. The synthesis of glutathione. Arch. of Biochem. a. Biophysics 47, 241–250 (1953).
Webster, G. C., and J. E. Varner: Peptide bond synthesis in higher plants. II. Studies on the mechanism of synthesis of γ-glutamyl cysteine. Arch. of Biochem. a. Biophysics 52, 21–32 (1954).
Peptide bond synthesis in higher plants. III. The formation of glutathione from γ-glutamyl cysteine. Arch. of Biochem. and Biophysics. 55, 95–103 (1955).
Weeks, D. C., and R. M. Robertson: Studies in the metabolism of plant cells. 8. Dependence of salt accumulation and salt respiration on the cytochrome system. Austral. J. Sci. Res. B 3, 487–500 (1950).
Weil-Malherbe, H., and R. H. Green: The catalytic of molybdate on the hydrolysis of organic phosphates. Biochemic. J. 49, 286–292 (1951).
Weinstein, L. H., and W. R. Robbins: The effect of different iron and manganese nutrient levels on the catalase and cytochrome oxidase activities of green and albino sunflower leaf tissues. Plant Physiol. 30, 27–32 (1955).
Weinstein, L. H., W, R. Robbins and W. W. Wainio: Assay of cytochrome oxidase activity of sunflower leaf tissue in relation to ph value and cation concentration of the buffer. Plant Physiol. 29, 388–409 (1954).
Wildman, E. G., and J. Bonner: The proteins of green leaves. I. Isolation, enzymatic properties and auxin content of spinach cytoplasmic proteins. Arch. of Biochem. 14, 381–413 (1947).
Winfield, M. E.: The role of boron in plant metabolism. II. An account of some attempts to isolate boron complexes from plant tissues. Austral. J. Exper. Biol. a. Med. Sci. 23, 111–117 (1945).
Wolfe, M.: The effect of molybdenum upon the nitrogen metabolism of Anabaena cylindrica. II. A more detailed study of molybdenum in nitrate assimilation. Ann. of Bot., N. S. 18, 309–325 (1954).
Wood, I. G., and P. M. Sibley: Carbonic anhydrase activity in plants in relation to zinc content. Austral. J. Sci. Res. B 5, 244–255 (1952).
Wosilait, W. D., and A. Nason: Pyridine nucleotide-quinone reductase. I. Purification and properties of the enzyme from pea seeds. J. of Biol. Chem. 206, 255–270 (1954).
Wosilait, W. D., A. Nason and A. J. Terrell: Pyridme nucleotidequinone reductase. II. Role in electron transport. J. of Biol. Chem. 206, 271–282 (1954).
Zittle, C. A.: Reaction of borate with substances of biological interest. Adv. Enzymol. 12, 493–527 (1951).
Zucker, M., and A. Nason: A pyridine nucleotide hydroxylamine reductase from Neurospora, J. of Biol. Chem. 213, 463–478 (1955).
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Hewitt, E.J. (1958). The role of mineral elements in the activity of plant enzyme systems. In: Adriani, M.J., et al. Die Mineralische Ernährung der Pflanze / Mineral Nutrition of Plants. Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology, vol 4. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-94729-2_18
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