Abstract
Mutant strains of the facultative autotrophic bacterium Alcaligenes eutrophus blocked in glycollate utilization were isolated and characterized. One of the strains, AE161, which lacked glycollate oxidoreductase activity, excreted up to 1.2μmol glycollate/mg cell protein per hour during autotrophic growth. This mutant strain was used to study the efficiency of CO2 fixation in terms of how much of the fixed carbon was excreted as glycollate under different conditions. Glycollate excretion was not detected during heterotrophic growth. Only 1% of the total CO2 fixed was excreted as glycollate in an atmosphere of 4% CO2 plus 20% O2. The rate of glycollate excretion showed a large increase and CO2 fixation decreased as the CO2 concentration was lowered. Almost half (40–50%) of the total CO2 fixed was excreted as glycollate in an atmosphere of 0.07% CO2 plus 20% O2.
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Abbreviations
- HPMS:
-
2-pyridyl-hydroxymethane sulphonic acid
- RuBP:
-
ribulose 1,5-bisphosphate
References
Andersen, K.: Mutations altering the catalytic activity of a plant-type ribulose biphosphate carboxylase/oxygenase in Alcaligenes eutrophus. Biochim. Biophys. Acta 585, 1–11 (1979)
Andersen, K., King, W. R., Valentine, R. C.: Catalytic mutants of ribulose bisphosphate carboxylase/oxygenase. In: Photosynthetic carbon assimilation (Siegelman, H. W., Hind, G., eds.), pp. 379–390. New York: Plenum Press 1978
Andrews, T. J., Lorimer, G. H.: Photorespiration: Still unavoidable? FEBS Lett. 90, 1–9 (1978)
Asami, S., Akazawa, T.: Biosynthetic mechanism of glycollate in Chromatium 6. Glycollate formation and metabolism under low O2. Plant Cell Physiol. 19, 1353–1361 (1978)
Badger, M. R., Andrews, T. J.: Effects of CO2 and O2, and temperature on a high affinity form of ribulose diphosphate carboxylase-oxygenase from spinach. Biochem. Biophys. Res. Commun. 60, 204–210 (1974)
Berry, J. A., Boynton, J., Kaplan, A., Badger, M. R.: Growth and photosynthesis of Chlamydomonas reinhardtii as a function of CO2 concentration. Carnegie Institute Yearbook 75, 423–432 (1976)
Bleiweis, A. S., Reeves, H. C., Ajl, S. J.: Rapid separation of some common intermediates of microbiol metabolism by thin-layer chromatography. Anal. Biochem. 20, 335–338 (1967)
Bowes, G., Ogren, W. L., Hageman, R. H.: Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase. Biochem. Biophys. Res. Commun. 45, 716–722 (1971)
Bowien, B., Mayer, F.: Further studies on the quaternary structure of d-ribulose-1,5-bisphosphate carboxylase from Alcaligenes eutrophus. Eur. J. Biochem. 88, 97–107 (1978)
Bowien, B., Mayer, F., Codd, G. A., Schlegel, H. G.: Purification, some properties, and quaternary structure of the d-ribulose-1,5-diphosphate carboxylase of Alcaligenes eutrophus. Arch. Microbiol. 110, 157–166 (1976)
Calkins, V. P.: Microdetermination of glycolic and oxalic acids. Ind. Engng. Chem. Anal. Ed. 15, 762–763 (1943)
Cheng, K. H., Miller, A. G., Colman, B.: An investigation of glycolate excretion in two species of blue-green algae. Planta (Berl.) 103, 110–116 (1972)
Chollet, R.: The biochemistry of photorespiration. Trends Biochem. Sci. 2, 155–159 (1977)
Codd, G. A., Bowien, B., Schlegel, H. G.: Glycollate production and excretion in Alcaligenes eutrophus. Arch. Microbiol. 110, 167–171 (1976)
Codd, G. A., Smith, B. M.: Glycollate formation and excretion by the purple photosynthetic bacterium Rhodospirillum rubrum. FEBS Lett. 48, 105–108 (1974)
Cohen, Y., de Jonge, I., Kuenen, J. G.: Excretion of glycolate by Thiobacillus neapolitanus grown in continuous culture. Arch. Microbiol. 122, 189–197 (1979)
Drews, G.: Untersuchungen zur Regulation der Bakteriochlorophyll-Synthese bei Rhodospirillum rubrum. Arch. Mikrobiol. 51, 186–198 (1965)
Döhler, G., Braun, F.: Untersuchung der Beziehung zwischen extracellulärer Glykolsäure-Ausscheidung und der photosynthetischen CO2-Aufnahme bei der Blaualge Anacystis nidulans. Planta (Berl.) 98, 357–361 (1971)
Halldal, P., Holmen, Aa. T.: The interrelationship between photosynthetic electron transport, glycolate excretion and amino acid metabolism in the blue-green alga Anacystis nidulans. Plant Cell Physiol. 20, 757–763 (1979)
Han, T.-W., Eley, J. H.: Glycolate excretion by Anacystis nidulans: Effect of bicarbonate concentration, oxygen concentration and light intensity. Plant Cell Physiol. 14, 285–291 (1973)
Jensen, R. G., Bahr, J. T.: Ribulose 1,5-bisphosphate carboxylaseoxygenase. Ann. Rev. Plant Physiol. 28, 379–400 (1977)
Ku, S. B., Edwards, G. E.: Oxygen inhibition of photosynthesis. I. Temperature dependence and relation to O2/CO2 solubility ratio. Plant Physiol. 59, 986–990 (1977a)
Ku, S. B., Edwards, G. E.: Oxygen inhibition of photosynthesis. II. Kinetic characteristics as affected by temperature. Plant Physiol. 59, 991–999 (1977b)
Kuehn, G. D., McFadden, B. A.: Ribulose 1,5-diphosphate carboxylase from Hydrogenomonas eutropha and Hydrogenomonas facilis. I. Purification, metallic ion requirements, inhibition, and kinetic constants. Biochemistry 8, 2394–2402 (1969a)
Kuehn, G. D., McFadden, B. A.: Ribulose 1,5-diphosphate carboxylase from Hydrogenomonas eutropha and Hydrogenomonas facilis. II. Molecular weight, subunits, composition, and sulfhydryl groups. Biochemistry 8, 2403–2408 (1969b)
Laing, W. A., Ogren, W. L., Hageman, R. H.: Regulation of soybean net photosynthetic CO2 fixation by the interaction of CO2, O2, and ribulose-1,5-diphosphate carboxylase. Plant Physiol. 54, 678–685 (1974)
Lord, J. M.: Glycolate oxidoreductase in Escherichia coli. Biochim. Biophys. Acta 267, 227–237 (1972)
Lorimer, G. H., Andrews, T. J., Tolbert, N. E.: Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action. Biochemistry 12, 18–23 (1973)
Lorimer, G. H., Krause, G. H., Berry, J. A.: The incorporation of [18O] oxygen into glycollate by intact chloroplasts. FEBS Lett. 78, 199–202 (1977)
Lorimer, G. H., Osmond, C. B., Akazawa, T., Asami, S.: On the mechanism of glycolate synthesis by Chromatium and Chlorella. Arch. Biochem. Biophys. 185, 49–56 (1978)
McFadden, B. A.: Assimilation of one-carbon compounds. In: The bacteria (Ornston, L. N., Sokatch, J. R., eds.), vol. 6, pp. 219–304. New York: Academic Press 1978
Nelson, E. B., Tolbert, N. E.: Glycolate dehydrogenase in green algae. Arch. Biochem. Biophys. 141, 102–110 (1970)
Purohit, K., McFadden, B. A.: Quaternary structure and oxygenase activity of d-ribulose-1,5-bisphosphate carboxylase from Hydrogenomonas eutropha. J. Bacteriol. 129, 415–421 (1977)
Reh, M., Schlegel, H. G.: Anreicherung und Isolierung autotropher Mutanten von Hydrogenomonas H16. Arch. Mikrobiol. 67, 99–109 (1969)
Repaske, R., Ambrose, C. A., Repaske, A. C., DeLacy, M. L.: Bicarbonate requirement for the elimination of the lag period of Hydrogenomonas eutropha. J. Bacteriol. 107, 712–717 (1971)
Schlegel, H. G., Kaltwasser, H., Gottschalk, G.: Ein Submersverfahren zur Kultur wasserstoffoxydierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38, 209–222 (1961)
Takabe, T., Osmond, C. B., Summons, R. E., Akazawa, T.: Effect of oxygen on photosynthesis and biosynthesis of glycolate in photoheterotrophically grown cells of Rhodospirillum rubrum. Plant Cell Physiol. 20, 233–241 (1979)
Tolbert, N. W.: Photorespiration. In: Algal physiology and biochemistry (Stewart, W. D. P., ed.), pp. 474–504. Oxford: Blackwell 1974
Vogels, G. D., van der Drift, C.: Differential analysis of glyoxylate derivatives. Anal. Biochem. 33, 143–157 (1970)
Zelitch, I.: The relationship of glycolic acid to respiration and photosynthesis in tobacco leaves. J. Biol. Chem. 234, 3077–3081 (1959)
Zelitch, I.: Improving the efficiency of photosynthesis. Science 188, 626–633 (1975)
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King, W.R., Andersen, K. Efficiency of CO2 fixation in a glycollate oxidoreductase mutant of Alcaligenes eutrophus which exports fixed carbon as glycollate. Arch. Microbiol. 128, 84–90 (1980). https://doi.org/10.1007/BF00422310
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DOI: https://doi.org/10.1007/BF00422310