The Activation of Enzymes with Light

  • Daniel H. Hug


Photoresponses have been described for bacteria, fungi, protozoa, algae, plants, invertebrates, and higher animals. These responses include phototaxis, phototropism, photomorphogenesis, photoperiodism, vision, and photocontrol of biological rhythms. The molecular details for the translation of a light stimulus to the observed biological response remain largely unknown for most responses to light. One possibility for the primary process in the stimulation of biological responses is the enhancement by light of an enzyme reaction. This can involve direct absorption of photons by an immediate component of the enzyme system (e.g., substrate), or indirect effects of light on enzymes such as the enhancement of protein synthesis, and enzyme activation which requires an additional protein acting as a light activation factor. The light activation of enzymes represents a topic that is developing rapidly, with particular emphasis in the areas of vision, photochromic enzyme inhibitors, photoreactivation, and enzyme activation in photosynthetic organisms. A few years ago there were not many reports on the activation of enzymes by light, whereas the photomactivation of enzymes has received widespread attention for years. Light activates specific enzymes, whereas inactivation by exposure to far-UV* radiation or by photodynamic action is not enzyme specific. Some inactivations by visible or near-UV light are selective, but are usually not reversible.


Action Spectrum Light Activation Euglena Gracilis Cyclic Nucleotide Phosphodiesterase Photoreceptor Membrane 
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  1. Acton, G. J., and Schöpfer, P., 1974, Phytochrome-induced synthesis of ribonuclease de novo in lupin hypocotyl sections, Biochem. J. 142:449–455.Google Scholar
  2. Altschule, M. D., (ed.), 1975, Frontiers of Pineal Physiology, Massachusetts Institute of Technology, Cambridge.Google Scholar
  3. Anderson, L. E., 1974, Activation of pea leaf chloroplast sedoheptulose-l,7-diphosphate phosphatase by light and dithiothreitol, Biochem. Biophys. Res. Commun. 59:907–913.Google Scholar
  4. Anderson, L. E., and Avron, M., 1976, Light modulation of enzyme activity in chloroplasts. Generation of membrane-bound vicinal-dithiol groups by photosynthetic electron transport, Plant Physiol. 57:209–213.Google Scholar
  5. Anderson, L. E., and Duggan, J. X., 1976, Light modulation of glucose-6-phosphate dehydrogenase. Partial characterization of the light inactivation system and its effects on the properties of the chloroplastic and cytoplasmic forms of the enzyme, Plant Physiol. 58:135–139.Google Scholar
  6. Anderson, L. E., and Lim, T., 1972, Chloroplast glyceraldehyde 3-phosphate dehydrogenase: Light-dependent change in the enzyme, FEBS Lett. 27:189–191.Google Scholar
  7. Aparicio, P. J., Roldán, J. M., and Calero, F., 1976, Blue light photoreactivation of nitrate reductase from green algae and higher plants, Biochem. Biophys. Res. Commun. 70:1071–1077.Google Scholar
  8. Apel, K., and Bogorad, L., 1976, Light-induced increase in the activity of maize plastid DNA-dependent RNA polymerase, Eur. J. Biochem. 67:615–620.Google Scholar
  9. Balasubramanian, D., Subramani, S., and Kumar, C., 1975, Modification of a model membrane structure by embedded photochrome, Nature (London) 254:252–254.Google Scholar
  10. Barrett, T. W., 1976, On the Comorosan effect, Physiol. Chem. Phys. 8:259–264.Google Scholar
  11. Bass, G. E., 1975, The Comorosan effect: Toward a perspective, Int. J. Quantum Chem., Quantum Biol. Symp. 2:321–324.Google Scholar
  12. Bass, G. E., and Chenevey, J. E., 1976, Irradiation induced rate enhancements for the LDH-pyruvate reaction, Int. J. Quantum Chem., Quantum Biol. Symp. 3:247–250.Google Scholar
  13. Bass, G. E., and Crisan, D., 1973, Concerning irradiation-induced biological activity alterations of tetracycline, Physiol. Chem. Phys. 5:331–335.Google Scholar
  14. Bass, G. E., Sandru, D., Chenevey, J. E., and Bucovaz, E. T., 1976, The Comorosan effect: Single- and double-blind studies on the urea/urease system, Physiol. Chem. Phys. 8:253–258.Google Scholar
  15. Baugher, J. F., and Grossweiner, L. I., 1975, Ultraviolet inactivation of papain, Photochem. Photobiol. 22:163–167.Google Scholar
  16. Berezin, I. V., Varfolomeyev, S. D., Klibanov, A. M., and Martinek, K., 1974, Light and ultrasonic regulation of α-chymotrypsin catalytic activity; proflavin as a light- and sound-sensitive competitive inhibitor, FEBS Lett. 39:329–331.Google Scholar
  17. Berger, T. J., and Orlando, J. A., 1973, Purification and some properties of a protein factor required for light-dependent transhydrogenase in Rhodopseudomonas spheroides, Arch. Biochem. Biophys. 159:25–31.Google Scholar
  18. Bersin, T., 1933, Uber die Einwirkung von Oxydations- und Reduktionsmitteln auf Papain. II. Die Aktivitätsbeeinflussung durch Licht, Organoarsenverbindungen und Ascorbinsäure, Hoppe-Seyler’s Z. Physiol. Chem. 222:177–186.Google Scholar
  19. Bieth, J., Vratsanos, S. M., Wassermann, N., and Erlanger, B. F., 1969, Photoregulation of biological activity by photochromic reagents, II. Inhibitors of acetylcholinesterase, Proc. Natl. Acad. Sci. USA 64:1103–1106.Google Scholar
  20. Bieth, J., Vratsanos, S. M., Wassermann, N. H., Cooper, A. G., and Erlanger, B. F., 1973, Photoregulation of biological activity by photochromic reagents. Inactivators of acetylcholinesterase, Biochemistry 12:3023–3027.Google Scholar
  21. Biscar, J. P., 1976, Photon enzyme activation, Bull. Math. Biol. 38:29–38.Google Scholar
  22. Bitensky, M. W., Miki, N., Keirns, J. J., Keirns, M., Baraban, J. M., Freeman, J., Wheeler, M. A., Lacy, J., and Marcus, F. R., 1975, Activation of photoreceptor disk membrane phosphodiesterase by light and ATP, Adv. Cyclic Nucleotide Res. 5:213–240.Google Scholar
  23. Bonting, S. L., Caravaggio, L. L., and Canady, M. R., 1964, Studies on sodium-potassium-activated adenosine triphosphatase X. Occurrence in retinal rods and relation to rhodopsin, Exp. Eye Res. 3:47–56.Google Scholar
  24. Bose, S. K., Gest, H., and Ormerod, J. G., 1961, Light-activated hydrogenase activity in a photosynthetic bacterium: A permeability phenomenon, J. Biol. Chem. 236:PC13–PC14.Google Scholar
  25. Bownds, D., Dawes, J., Miller, J., and Stahlman, M., 1972, Phosphorylation of frog photoreceptor membranes induced by light, Nature (London), New Biol. 237:125–127.Google Scholar
  26. Brodie, A. E., and Bownds, D., 1976, Biochemical correlates of adaptation processes in isolated frog photoreceptor membranes, J. Gen. Physiol. 68:1–11.Google Scholar
  27. Buchanan, B. B., and Wolosiuk, R. A., 1976, Photosynthetic regulatory protein found in animal and bacterial cells, Nature (London) 264:669–670.Google Scholar
  28. Buchanan, B. B., Schürmann, P., and Kalberer, P. P., 1971, Ferredoxin-activated fructose diphosphatase of spinach chloroplasts, J. Biol. Chem. 246:5952–5959.Google Scholar
  29. Carell, E. F., Egan, J. M. and Pratt, E. A., 1970, Studies on chloroplast development and replication in Euglena, II. Identification of two different deoxyribonucleases. Arch. Biochem. Biophys. 138:26–31.Google Scholar
  30. Castle, E. S., 1966, A kinetic model for adaptation and the light responses of Phycomyces, J. Gen. Physiol. 49:925–935.Google Scholar
  31. Chader, G. J., Herz, L. R., and Fletcher, R. T., 1974, Light activation of phosphodiesterase activity in retinal rod outer segments, Biochim. Biophys. Acta 347:491–493.Google Scholar
  32. Chader, G. J., Fletcher, R. T., O’Brien, P. J., and Krishna, G., 1976, Differential phosphorylation by GTP and ATP in isolated rod outer segments of the retina, Biochemistry 15:1615–1620.Google Scholar
  33. Champigny, M., and Bismuth, E., 1976, Role of photosynthetic electron transfer in light activation of Calvin cycle enzymes, Physiol. Plant. 36:95–100.Google Scholar
  34. Chollet, R., and Anderson, L. L., 1976, Regulation of ribulose 1,5-bisphosphate carboxylase-oxygenase activities by temperature pretreatment and chloroplast metabolites, Arch. Biochem. Biophys. 176:344–351.Google Scholar
  35. Cohen, R. J., 1974, Cyclic AMP levels in Phycomyces during a response to light, Nature (London) 251:144–146.Google Scholar
  36. Comorosan, S., 1975, The measurement process in biological systems: A new phenomenology, J. Theor. Biol. 51:35–49.Google Scholar
  37. Comorosan, S., Cru, M., and Vieru, S., 1972, The interaction between enzymic systems and irradiated substrates, Enzymologia 42:31–43.Google Scholar
  38. Cook, J. S., 1970, Photoreactivation in animal cells, in: Photophysiology, Vol. 5 (A. C. Giese, ed.), pp. 191–233, Academic Press, New York.Google Scholar
  39. Cummings, F. W., 1975, A biochemical model of the circadian clock, J. Theor. Biol. 55:455–470.Google Scholar
  40. Dever, D. F., and Grunwald, E., 1976, Megawatt infrared laser chemistry of CCIF3 and CCI3F. 1. Photochemistry, photophysics, and effect of H2,J. Am. Chem. Soc. 98:5055–5062.Google Scholar
  41. Diamond, J., Schiff, J. A., and Kelner, A., 1975, Photoreactivating enzyme from Euglena and the control of its intracellular level, Arch. Biochem. Biophys. 167:603–614.Google Scholar
  42. Dose, K., and Risi, S., 1972, The action of U.V. light of various wavelengths on papain, Photochem. Photobiol. 15:43–50.Google Scholar
  43. Ebrey, T. G., and Honig, B., 1975, Molecular aspects of photoreceptor function, Q. Rev. Biophys. 8:129–184.Google Scholar
  44. Egan, J. M., and Carell, E. F., 1972, Studies on chloroplast development and replication in Euglena. III. A study of the site of synthesis of alkaline deoxyribonuclease induced during chloroplast development in Euglena gracilis, Plant Physiol. 50:391–395.Google Scholar
  45. Engelsma, G., 1974, On the mechanism of the changes in phenylalanine ammonia-lyase activity induced by ultraviolet and blue light in gherkin hypocotyls, Plant Physiol. 54:702–705.Google Scholar
  46. Erlanger, B. F., 1976, Photoregulation of biologically active macromolecules, Ann. Rev. Biochem. 45:267–283.Google Scholar
  47. Errera, M., 1953, Mechanisms of biological action of ultraviolet and visible radiations, Prog. Biophys. Biophys. Chem. 3:88–130.Google Scholar
  48. Evans, A., and Smith, H., 1976, Spectrophotometric evidence for the presence of phytochrome in the envelope membranes of barley etioplasts, Nature (London) 259:323–325.Google Scholar
  49. Feldman, J. F., 1975, Circadian periodicity in Neurospora: Alteration by inhibitors of cyclic AMP phosphodiesterase, Science 190:789–790.Google Scholar
  50. Fletcher, R. T., and Chader, G. J., 1976, Cyclic GMP: Control of concentration by light in retinal photoreceptors, Biochem. Biophys. Res. Commun. 70:1297–1302.Google Scholar
  51. Frank, R. N., and Buzney, S. M., 1975, Mechanism and specificity of rhodopsin phosphorylation, Biochemistry 14:5110–5117.Google Scholar
  52. Frank, R. N., and Goldsmith, T. H., 1965, Adenosine triphosphatase activity in the rod outer segments of the pig’s retina, Arch. Biochem. Biophys. 110:517–525.Google Scholar
  53. Galston, A. W., 1974, Plant photobiology in the last half century, Plant Physiol. 54:427–436.Google Scholar
  54. Goodwin, B. C., and Vieru, S., 1975, Low energy electromagnetic perturbation of an enzyme substrate, Physiol. Chem. Phys. 7:89–90.Google Scholar
  55. Hahlbrock, K., 1976, Regulation of phenylalanine ammonia-lyase activity in cell-suspension cultures of Petroselinum hortense, Eur. J. Biochem. 63:137–145.Google Scholar
  56. Hahlbrock, K., Knobloch, K., Kreuzaler, F., Potts, J. R. M., and Wellman, E., 1976, Coordinated induction and subsequent activity changes of two groups of metabolically interrelated enzymes, Eur. J. Biochem. 61:199–206.Google Scholar
  57. Halberstam, M. A., and Gordin, M. B., 1973, Kinetics of reversible photochrome reactions in the series of 1,5-disubstituted 3,3-dimethyl-6′-nitro-8′-bromospiro-[(2′H, 1′-benzopyran)-2,2′-indolines], Photochem. Photobiol. 17:103–113.Google Scholar
  58. Halldal, P., and Taube, O., 1972, Ultraviolet action and photoreactivation in algae, in: Photophysiology, Vol. 7 (A. C. Giese, ed.), pp. 163–188, Academic Press, New York.Google Scholar
  59. Hanawalt, P. C., and Setlow, R. B., (eds.), 1975, Molecular Mechanisms for the Repair of DNA, Plenum Press, New York.Google Scholar
  60. Hanson, R. S., 1964, Light-activated hydrogenase in Rhodospirillum rubrum, Biochim. Biophys. Acta 79:433–445.Google Scholar
  61. Harm, H., 1976, Repair of UV-irradiated biological systems: Photoreactivation, in: Photochemistry and Photobiology of Nucleic Acids, Vol. 2, Biology (S. Y. Wang, ed.), pp. 219–263, Academic Press, New York.Google Scholar
  62. Harm, H., and Rupert, C. S., 1976, Analysis of photoenzymatic repair of UV lesions in DNA by single light flashes. XI. Light-induced activation of the yeast photoreactivating enzyme, Mutation Res. 34:75–92;Google Scholar
  63. Harm, W., Rupert, C. S., and Harm, H., 1971, The study of photoenzymatic repair of UV lesions in DNA by flash photolysis, in: Photophysiology, Vol. 6 (A. C. Giese, ed.), pp. 279–324, Academic Press, New York.Google Scholar
  64. Hatch, M. D., and Slack, C. R., 1969, Studies on the mechanism of activation and inactivation of pyruvate, phosphate dikinase, Biochem. J. 112:549–558.Google Scholar
  65. Heinrich, M. R., and Lanyi, J. K., 1977, Light energy transduction by the purple membrane of halophilic bacteria, Fed. Proc. 36:1797–1839.Google Scholar
  66. Hendricks, S. B., 1964, Photochemical aspects of plant photoperiodicity, in: Photophysiology Vol. 1 (A. C. Giese, ed.), pp. 305–331, Academic Press, New York.Google Scholar
  67. Hendricks, S. B., and Borthwick, H. A., 1967, The function of phytochrome in regulation of plant growth, Proc. Natl. Acad. Sci. USA 58:2125–2130.Google Scholar
  68. Hillman, W. S., 1967, The physiology of phytochrome, Plant Physiol. 18:301–324.Google Scholar
  69. Hug, D. H., and Hunter, J. K., 1970, Photoactivation of urocanase in Pseudomonas putida: Possible role in photoregulation of histidine metabolism, J. Bacteriol. 102:874–876.Google Scholar
  70. Hug, D. H., and Roth, D., 1971, Photoactivation of urocanase in Pseudomonas putida. Purification of inactive enzyme, Biochemistry 10:1397–1402.Google Scholar
  71. Hug, D. H., Hunter, J. K., and Roth, D. E., 1971, Photoactivation of urocanase in Pseudomonas putida: factors influencing activation, Photochem. Photobiol. 13:171–177.Google Scholar
  72. Hug, D. H., O’Donnell, P. S., and Hunter, J. K., 1976, Activation of urocanase by ultraviolet light, Abstr. Amer. Soc. Photobiol., p. 42.Google Scholar
  73. Jaffe, M. J., 1970, Evidence for the regulation of phytochrome-mediated processes in bean roots by the neurohumor, acetylcholine, Plant Physiol. 46:768–777.Google Scholar
  74. Jagger, J., and Stafford, R. S., 1965, Evidence for two mechanisms of photoreactivation in Escherichia coli B, Biophys. J. 5:75–88.Google Scholar
  75. Johnson, H. S., 1971, NADP-malate dehydrogenase: Photoactivation in leaves of plants with Calvin cycle photosynthesis, Biochem. Biophys. Res. Commun. 43:703–709.Google Scholar
  76. Johnson, H. S., and Hatch, M. D., 1970, Properties and regulation of leaf nicotinamide adenine dinucleotide phosphate-malate dehydrogenase and ‘malic’ enzyme in plants with the d-dicarboxylic acid pathway of photosynthesis, Biochem. J. 119:273–280.Google Scholar
  77. Johnson, J. H., Reed, B. C., and Rilling, H. C., 1974, Early photoinduced enzymes of photoinduced carotenogenesis in a Mycobacterium species, J. Biol. Chem. 249:402–406.Google Scholar
  78. Jones-Lecointe, A., Rose, S. P. R., and Sinha, A. K., 1976, Sub-cellular localization of enhanced lysine incorporation into cerebral cortex proteins in dark-reared and light-exposed rats,J. Neurochem. 26:929–933.Google Scholar
  79. Karube, I., Nakamoto, Y., Namba, K., and Suzuki, S., 1976, Photocontrol of urease-collagen membrane activity, Biochim. Biophys. Acta 429:975–981.Google Scholar
  80. Kaufman, H., Vratsanos, S. M., and Erlanger, B. F., 1968, Photoregulation of an enzymic process by means of a light-sensitive ligand, Science 162:1487–1488.Google Scholar
  81. Keilin, D., and Hartree, E. F., 1955, Cyanide compounds of ferroperoxidase and myoglobin and their reversible photodissociation, Biochem. J. 61:153–171.Google Scholar
  82. Keirns, J. J., Miki, N., Bitensky, M. W., and Keirns, M., 1975, A link between rhodopsin and disc membrane cyclic nucleotide phosphodiesterase. Action spectrum and sensitivity to illumination, Biochemistry 14:2760–2766.Google Scholar
  83. Keister, D. L., and Yike, N. J., 1966, Studies on an energy-linked pyridine nucleotide transhy-drogenase in photosynthetic bacteria. I. Demonstration of the reaction in Rhodospirillum rubrum, Biochem. Biophys. Res. Commun. 24:519–525.Google Scholar
  84. Kelly, G. J., Zimmermann, G., and Latzko, E., 1976, Light induced activation of fructose-1,6-biphosphatase in isolated intact chloroplasts, Biochem. Biophys. Res. Commun. 70:193–199.Google Scholar
  85. Kelner, A., 1969, Biological aspects of ultraviolet damage, photoreactivation and other repair systems in microorganisms, in: The Biologic Effects of Ultraviolet Radiation (F. Urbach, ed.), pp. 77–82,Google Scholar
  86. Pergamon, Oxford, Kimmel, J. R., and Smith, E. L., 1954, Crystalline papain. I. Preparation, specificity and activation,J. Biol. Chem. 207:515–531.Google Scholar
  87. Kowallik, W., and Ruyter, G., 1976, Über Aktivitätssteigerungen der Pyruvatkinase durch Blaulicht oder Glucose bei einer Chlorophyllfreien Chlorella-Mutante, Planta 128:11–14.Google Scholar
  88. Kühn, H., and Dreyer, W. J., 1972, Light dependent phosphorylation of rhodopsin by ATP, FEBS Lett. 20:1–6.Google Scholar
  89. Kühn, H., Cook, J. H., and Dreyer, W. J., 1973, Phosphorylation of rhodopsin in bovine photoreceptor membranes. A dark reaction after illumination, Biochemistry 12:2495–2502.Google Scholar
  90. Lorimer, G. H., Badger, M. R., and Andrews, T. J., 1976, The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications, Biochemistry 15:529–536.Google Scholar
  91. Martinek, K., Varfolomeyev, S. D., and Berezin, I. V., 1971, Interaction of α-chymotrypsin with N-cinnamoylimidazole; substrate sensitive to light, Eur. J. Biochem. 19:242–249.Google Scholar
  92. McConnell, D. G., and Scarpelli, D. G., 1963, Rhodopsin: An enzyme, Science 139:848.Google Scholar
  93. Menaker, M. (ed.), 1976, Extraretinal photoreception. Symposium on extraretinal photoreception in circadian rhythms and related phenomena, Photochem. Photobiol. 23:213–306.Google Scholar
  94. Menger, E. L. (ed.), 1975, Special issue on the chemistry of vision, Accounts Chem. Res. 8:81–112.Google Scholar
  95. Miki, N., Keirns, J. J., Marcus, F. R., Freeman, J., and Bitensky, M. W., 1973, Regulation of cyclic nucleotide concentrations in photoreceptors: An ATP-dependent stimulation of cyclic nucleotide phosphodiesterase by light, Proc. Natl. Acad. Sci. USA 70:3820–3824.Google Scholar
  96. Miki, N., Keirns, J. J., Marcus, F. R., and Bitensky, M. W., 1974, Light regulation of adenosine 3′,5′ cyclic monophosphate levels in vertebrate photoreceptors, Exp. Eye Res. 18:281–297.Google Scholar
  97. Miller, W. H., Gorman, R. E., and Bitensky, M. W., 1971, Cyclic adenosine monophosphate: function in photoreceptors, Science 174:295–297.Google Scholar
  98. Mitrakos, K., and Shropshire, W., Jr. (eds.), 1972, Phytochrome, Academic Press, New York.Google Scholar
  99. Montagnoli, G., 1974, Azoaldolase. Photochrome enzyme, Acta Vitaminol. Enzymol. 28:268–285.Google Scholar
  100. Montagnoli, G., Monti, S., Nannicini, L., and Felicioli, R., 1976, Azoaldolase photosensitivity, Photochem. Photobiol. 23:29–32.Google Scholar
  101. Namba, K., and Suzuki, S., 1975, Photo-control of enzyme activity with a photochromic spiropyran compound, modification of α-amylase with spiropyran compound, Chem. Lett. 1975:947–950.Google Scholar
  102. Oishi, T., and Lauber, J. K., 1973, Effect of light and darkness on pineal hydroxymethyl-O-methyl transferase (HIOMT) in Japanese quail, Life Sciences 13:1105–1116.Google Scholar
  103. Orlando, J. A., 1970, Involvement of sulfhydryl groups in light-dependent transhydrogenase of Rhodopseudomonas spheroides, Arch. Biochem. Biophys. 141:111–120.Google Scholar
  104. Page, R. M., 1968, Phototropism in fungi, in: Photophysiology, Vol. 3 (A. C. Giese, ed.), pp. 65–90, Academic Press, New York.Google Scholar
  105. Paine, A. J., 1976, Induction of benzo[a]pyrene mono-oxygenase in liver cell culture by the photochemical generation of active oxygen species, Biochem. J. 158:109–117.Google Scholar
  106. Pavlidis, T., and Kauzmann, W., 1969, Toward a quantitative biochemical model for circadian oscillators, Arch. Biochem. Biophys. 132:338–348.Google Scholar
  107. Purec, L., and Krasna, A. I., 1967, The activation of the hydrogenase of Proteus vulgaris by visible light, Proc. Natl. Acad. Sci. USA 57:1416–1421.Google Scholar
  108. Puree, L., and Krasna, A. I., 1968, The effect of ultraviolet light on the hydrogenase of Proteus vulgaris, Biochemistry 7:51–55.Google Scholar
  109. Puree, L., Krasna, A. I., and Rittenberg, D., 1962, The inhibition of hydrogenase by carbonmonoxide and the reversal of this inhibition by light, Biochemistry 1:270–275.Google Scholar
  110. Robb, R. M., 1974, Histochemical evidence of cyclic nucleotide phosphodiesterase in photoreceptor outer segments, Invest. Opthalmol. 13:740–747.Google Scholar
  111. Roth, D., and Hug, D. H., 1972, Photoactivation of urocanase in Pseudomonas putida: Action spectrum, Radiat. Res. 50:94–104.Google Scholar
  112. Rupert, C. S., 1964, Photoreactivation of ultraviolet damage, in: Photophysiology, Vol. 2 (A. C. Giese, ed.), pp. 283–327, Academic Press, New York.Google Scholar
  113. Rupert, C. S., and To, K., 1976, Substrate dependence of the action spectrum for photoenzy-matic repair of DNA, Photochem. Photobiol. 24:229–235.Google Scholar
  114. Sadana, J. C., and Rittenberg, D., 1963, Some observations on the enzyme hydrogenase of Desulfovibrio desulfuricans, Proc. Natl. Acad. Sci. USA 50:900–904.Google Scholar
  115. Schengrund, C., and Krasna, A. I., 1969, Purification and properties of the light-activated hydrogenase of Proteus vulgaris, Biochim. Biophys. Acta 185:332–337.Google Scholar
  116. Schrauzer, G. N., Katz, R. N., Grate, J. H., and Vickrey, T. M., 1976, Photochemical induction of enzymatic activity of a carbocyclic analog of coenzyme B12: A contribution to the elucidation of the mechanism of action of coenzyme B12, Angew. Chem. (Int. Ed. Engl.) 15:170–171.Google Scholar
  117. Schröder, J., Betz, B., and Hahlbrock, K., 1976, Light-induced enzyme synthesis in cell suspension cultures of Petroselinum hortense, Eur. J. Biochem. 67:527–541.Google Scholar
  118. Schürmann, P., Wolosiuk, R. A., Breazeale, V. D., and Buchanan, B. B., 1976, Two proteins function in the regulation of photosynthetic CO2 assimilation in chloroplasts, Nature (London) 263:257–258.Google Scholar
  119. Semler, B. L., Hodson, R. C., Williams, S. K., II, and Howell, S. H., 1975, The induction of allophanate lyase during the vegetative cell cycle in light-synchronized cultures of Chlamy-domonas reinhardi, Biochim. Biophys. Acta 399:71–78.Google Scholar
  120. Setlow, J. K., 1966, The molecular basis of biological effects of ultraviolet radiation and photoréactivation, in: Current Topics in Radiation Research, Vol. 3 (M. Ebert and A. Howard, eds.), pp. 197–248, North-Holland, Amsterdam.Google Scholar
  121. Sherman, R. L., Siebert, S. T., and Yee, W. H., 1973, A note on the effect of electromagnetic field on enzymic substrates, Physiol. Chem. Phys. 5:49–56.Google Scholar
  122. Shugar, D., 1951, Ultra-violet irradiation of triosephosphate dehydrogenase, Biochim. Biophys. Acta 6:548–561.Google Scholar
  123. Sisson, T. R. C., 1976, Visible light therapy of neonatal hyperbilirubinemia, in: Photochemical and Photobiological Reviews, Vol. 1 (K. C. Smith, ed.), pp. 241–268, Plenum Press, New York.Google Scholar
  124. Small, G. D., and Sturgen, R. S., 1976, Purification and properties of a light-inducible nuclease from Euglena gracilis, Nucleic Acids Res. 3:1277–1293.Google Scholar
  125. Smith, H., 1975, Phytochrome and Photomorphogenesis, McGraw-Hill, New York.Google Scholar
  126. Smith, H., Attridge, T. H., and Johnson, C. B., 1976, Photocontrol of enzyme activity, in: Perspectives in Experimental Biology, Vol. 2 (N. Sunderland, ed.), pp. 325–336, Pergamon, New York.Google Scholar
  127. Sutherland, J. C., and Sutherland, B. M., 1975, Human photoreactivating enzyme, Action spectrum and safelight conditions, Biophys. J. 15:435–440.Google Scholar
  128. Tezuka, T., and Yamamoto, Y., 1972, Photoregulation of nicotinamide adenine dinucleotide kinase activity in cell-free extracts, Plant Physiol. 50:458–462.Google Scholar
  129. Tezuka, T., and Yamamoto, Y., 1974, Kinetics of activation of nicotinamide adenine dinucleotide kinase by phytochrome—far red-absorbing form, Plant Physiol. 53:717–722.Google Scholar
  130. Tezuka, T., and Yamamoto, Y., 1975, Photoactivation of NAD kinase through phytochrome. Phosphate donors and cofactors, Plant Physiol. 56:728–730.Google Scholar
  131. Turek, F. W., McMillan, J. P., and Menaker, M., 1976, Melatonin: Effects on circadian locomotor rhythm of sparrows, Science 194:1441–1443.Google Scholar
  132. Varfolomeyev, S. D., Klibanov, A. M., Martinek, K., and Berezin, I. V., 1971, Light-initiated enzymic activity caused by photostereoisomerization of cis-4-nitrocinnamoyl-α-chymotrypsin, FEBS Lett. 15:118–120.Google Scholar
  133. Vince-Prue, D., 1975, Photoperiodism in Plants, McGraw-Hill, London.Google Scholar
  134. Volotovskii, I. D., Voskresenskaya, L. G., and Konev, S. V., 1972, Possibility of conformational activation of the enzyme-substrate complex of aldolase by ultraviolet radiation, Biofizika 17:971–977;Google Scholar
  135. Volotovskii, I. D., Voskresenskaya, L. G., and Konev, S. V., 1972, Possibility of conformational activation of the enzyme-substrate complex of aldolase by ultraviolet radiation, Biophysics 17:1018–1024.Google Scholar
  136. Wainberg, M. A., and Erlanger, B. F., 1971, Investigation of the active center of trypsin using photochromic substrates, Biochemistry 10:3816–3819.Google Scholar
  137. Wainwright, S. D., 1975, Effects of changes in environmental lighting upon levels of hydroxyindole-O-methyltransferase activity in the developing-chick pineal gland. Can. J. Biochem. 53:438–443.Google Scholar
  138. Wald, G., 1956, The biochemistry of visual excitation, in: Enzymes: Units of Biological Structure and Function (O. H. Gaebler, ed.), pp. 355–367, Academic Press, New York.Google Scholar
  139. Wald, G., 1965, Visual excitation and blood clotting, Science 150:1028–1030.Google Scholar
  140. Wald, G., 1968, Molecular basis of visual excitation, Science 162:230–239.Google Scholar
  141. Wang, S. Y., (ed.), 1976, Photochemistry and Photobiology of Nucleic Acids, Vol. 2, Biology, Academic Press, New York.Google Scholar
  142. Warburg, O., and Negelein, E., 1928, Über die photochemische Dissoziation bei intermittierender Belichtung und das absolute Absorptionsspektrum des Atmungsferments, Biochem. Z. 202:202–228.Google Scholar
  143. Weeks, O. B., Saleh, F. K., Wirahadikusumah, M., and Berry, R. A., 1973, Photoregulated carotenoid biosynthesis in non-photosynthetic microorganisms, Pure Appl. Chem. 35:63–80.Google Scholar
  144. Weller, M., Goridis, C., Virmaux, N., and Mandel, P., 1975a, A hypothetical model for the possible involvement of rhodopsin phosphorylation in light and dark adaptation in the retina, Exp. Eye Res. 21:405–408.Google Scholar
  145. Weiler, M., Virmaux, N., and Mandel, P., 1975b, Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin, Proc. Natl. Acad. Sci. USA 72:381–385.Google Scholar
  146. Weiler, M., Virmaux, N., and Mandel, P., 1975c, Role of light and rhodopsin phosphorylation in control of permeability of retinal rod outer segment disk to Ca2+, Nature (London) 256:68–70.Google Scholar
  147. Weiler, M., Virmaux, N., and Mandel, P., 1976, The relative specificity of opsin kinase towards ATP and GTP and the lack of effect of cyclic nucleotides on the activity of the enzyme, Exp. Eye Res. 23:65–67.Google Scholar
  148. White, E. H., Miano, J. D., Watkins, C. J., and Breaux, E. J., 1974, Chemically produced excited states, Angew. Chem. (Int. Ed. Engl.) 13:229–243.Google Scholar
  149. Wildner, G. F., and Criddle, R. S., 1969, Ribulose diphosphate carboxylase I. A factor involved in light activation of the enzyme, Biochem. Biophys. Res. Commun. 37:952–960.Google Scholar
  150. Windorfer, A., Jr., Faxelius, G., and Boréus, L. O., 1975, Studies on phototherapy in newborn infants, Acta Paediatr. Scand. 64:293–298.Google Scholar
  151. Wun, K. L., Gih, A., and Sutherland, J. C., 1977, Photoreactivating enzyme from Escherichia coli: Appearance of new absorption on binding to ultraviolet irradiated DNA, Biochemistry 16:921–924.Google Scholar
  152. Wurtman, R. J., Axelrod, J., and Kelly, D. E., 1968, The Pineal, Academic Press, New York.Google Scholar
  153. Yeary, R. A., Wise, K. J., and Davis, D. R., 1975, Activation of hepatic microsomal glu-curonyltransferase from Gunn rats by exposure to light, Life Sciences 17:1887–1890.Google Scholar
  154. Zimmermann, W. F., Daemen, F. J. M., and Bonting, S. L., 1976, Distribution of enzyme activities in subcellular fractions of bovine retina,J. Biol. Chem. 251:4700–4705.Google Scholar
  155. Zöllner, E. J., Weinblum, D., Obermeier, J., and Zahn, R. K., 1976, Influence of UV irradiation, 4-nitroquinoline-l-oxide, methylmethanesulfonate, and bleomycin on the activity of an alkaline deoxyribonuclease from human lymphocytes, Exp. Cell Res. 99:185–189.Google Scholar
  156. Zucker, M., 1972, Light and enzymes, Ann. Rev. Plant Physiol. 23:133–156.Google Scholar
  157. Zurzycki, J., 1972, Primary reactions in the chloroplast rearrangements, Acta Protozool. 11:189–199.Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Daniel H. Hug
    • 1
    • 2
  1. 1.Bacteriology Research LaboratoryVeterans Administration HospitalIowa CityUSA
  2. 2.Department of Internal MedicineUniversity of IowaIowa CityUSA

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