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Activation of ribulose-1,5-bisphosphate carboxylase by chloroplast metabolites in a reconstituted spinach chloroplast system

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Abstract

In a preparation of soluble components from isolated spinach (Spinecia oleracea L.) chloroplasts, the activity of ribulose-1,5-bisphosphate carboxylase (EC 4.1.1.39) is strongly increased by 6-phosphogluconate or by NADPH at pH 8.0. When the thylakoid system is added to these soluble components (reconstituted chloroplast system) plus ferredoxin, the carboxylase is even more strongly activated in the light. This “light” activation appears to be due to reduction of endogenous NADP+ by electrons from the light reactions transferred via ferredoxin, since NADPH alone can activate the purified enzyme in the dark while reduced ferredoxin does not. The regulatory properties of the enzyme in the reconstituted chloroplast system are compared with those of the isolated enzyme, and their possible physiologic significance is discussed.

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Abbreviations

Fd:

ferredoxin

PPC:

pentose phosphate cycle

6-PGluA:

6-phosphogluconate

Rib-5-P:

ribose-5-phosphate

RuBP:

ribulose-1,5-bisphosphate

References

  • Anderson, L.E., Avron, M.: Light modulation of enzyme activity in chloroplasts. Generation of membrane-bound vicinal-dithiol groups by photosynthetic electron transport. Plant Physiol. 57, 209–213 (1976)

    Google Scholar 

  • Bahr, J.T., Jensen, R.G.: Ribulose diphosphate carboxylase from freshly ruptured spinach chloroplasts having an in vivo Km (CO2). Plant Physiol. 53, 39–44 (1974)

    Google Scholar 

  • Bassham, J.A., Krause, G.H.: Free energy changes and metabolic regulation in steady-state photosynthetic carbon reduction. Biochim. Biophys. Acta 189, 207–221 (1969)

    Google Scholar 

  • Bassham, J.A., Levine, G., Forger, J.: Photosynthesis in vitro. Plant Sci. Lett. 2, 15–21, (1974)

    Google Scholar 

  • Chollet, R., Anderson, L.L.: Regulation of ribulose-1,5-bisphosphate carboxylase-oxygenase activities by temperature pretreatment and chloroplast metabolites. Arch. Biochem. Biophys. 176, 344–351 (1976)

    Google Scholar 

  • Chu, D.K., Bassham, J.A.: Activation and inhibition of ribulose-1,5-diphosphate carboxylase by 6-phosphogluconate. Plant Physiol. 52, 373–379 (1973)

    Google Scholar 

  • Chu, D.K., Bassham, J.A.: Activation and inhibition of ribulose-1,5-diphosphate carboxylase by nicotinamide adenine dinucleotide, phosphate and other chloroplast metabolites. Plant Physiol. 54, 556–559 (1974)

    Google Scholar 

  • Chu, D.K., Bassham, J.A.: Regulation of ribulose-1,5-diphosphate carboxylase by substrates and other metabolites. Plant Physiol. 55, 720–726 (1975)

    Google Scholar 

  • Heldt, H.W., Werdan, K., Milovancev, M., Geller, G.: Alkalization of the chloroplast stroma caused by light-dependent proton flux into the thylakoid space. Biochim. Biophys. Acta 314, 224–241 (1973)

    Google Scholar 

  • Jensen, R.G., Bassham, J.A.: Photosynthesis by isolated chloroplasts. Proc. Nat. Acad. Sci. (U.S.A.) 56, 1095–1101 (1966)

    Google Scholar 

  • Lendzian, K.J., Ziegler, H.: Über die Regulation der Glucose-6-phosphat-Dehydrogenase in Spinatchloroplasten durch Licht. Planta 94, 27–36 (1970)

    Google Scholar 

  • Lendzian, K.J., Bassham, J.A.: Regulation of glucose-6-phosphate dehydrogenase in spinach chloroplasts by ribulose-1,5-diphosphate and NADPH/NADP+ ratios. Biochim. Biophys. Acta 396, 260–275 (1975)

    Google Scholar 

  • Lendzian, K.J., Bassham, J.A.: NADPH/NADP+ ratios in photosynthesizing reconstituted chloroplasts. Biochim. Biophys. Acta 430, 478–489 (1976)

    Google Scholar 

  • Lilley, R.McC., Walker, D.A.: An improved spectrophotometric assay for ribulosebisphosphate carboxylase. Biochim. Biophys. Acta 358, 226–229 (1974)

    Google Scholar 

  • Lorimer, G.H., Badger, M.R., Andrews, T.J.: The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. Biochem. 15, 529–536 (1976)

    Google Scholar 

  • Platt, S.G., Plaut, Z., Bassham, J.A.: Analysis of steady-state photosynthesis in alfalfa leaves. Plant Physiol. 57, 69–73 (1976)

    Google Scholar 

  • Pon, N.G., Rabin, B.R., Calvin, M.: Mechanism of the carboxydismutase reaction. I. The effect of preliminary incubation of substrates, metal ion, and enzyme on activity. Biochem. Z. 338, 7–19 (1963)

    Google Scholar 

  • Vernon, L.P.: Spectrophotometric determination of chlorophylls and pheophytins in plant extracts. Anal. Chem. 32, 1144–1150 (1960)

    Google Scholar 

  • Walker, D.A., McCormick, A.V., Stokes, D.M.: CO2-dependent oxygen evolution by envelope-free chloroplasts. Nature 233, 346–347 (1971)

    Google Scholar 

  • Wolosiuk, R.A., Buchanan, B.B.: Thioredoxin and glutathione regulate photosynthesis in chloroplasts. Nature 266, 565–567 (1977)

    Google Scholar 

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Lendzian, K.J. Activation of ribulose-1,5-bisphosphate carboxylase by chloroplast metabolites in a reconstituted spinach chloroplast system. Planta 143, 291–296 (1978). https://doi.org/10.1007/BF00392001

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  • DOI: https://doi.org/10.1007/BF00392001

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