Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Feb;68(2):464–468. doi: 10.1073/pnas.68.2.464

Interactions between ADP and the Coupling Factor of Photophosphorylation

Harry Roy 1, Evangelos N Moudrianakis 1
PMCID: PMC388961  PMID: 5277102

Abstract

The coupling factor of photophosphorylation, which carries out the terminal steps in the light-dependent synthesis of ATP in spinach chloroplasts, forms tight complexes with [14C]ADP in vitro. The bound [14C]ADP undergoes a transphosphorylation reaction to give [14C]AMP and [14C]ATP. The [14C]ATP remains tightly bound, and can be recovered conveniently only by denaturation of the enzyme nucleotide complex. If spinach membranes are illuminated in the presence of pyocyanine and [3H]AMP or [32P]Pi, the enzyme can be recovered as a tight complex with [3H]ADP or [32P]ADP. The evidence indicates that AMP is an earlier acceptor of phosphate than is ADP, in a light-driven phosphorylation reaction. It also suggests that AMP serves as a cofactor in photophosphorylation.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AVRON M. Photophosphorylation by swiss-chard chloroplasts. Biochim Biophys Acta. 1960 May 20;40:257–272. doi: 10.1016/0006-3002(60)91350-0. [DOI] [PubMed] [Google Scholar]
  2. Bennun A., Racker E. Partial resolution of the enzymes catalyzing photophosphorylation. IV. Interaction of coupling factor 1 from chloroplasts with components of the chloroplast membrane. J Biol Chem. 1969 Mar 10;244(5):1325–1331. [PubMed] [Google Scholar]
  3. Hind G., Jagendorf A. T. SEPARATION OF LIGHT AND DARK STAGES IN PHOTOPHOSPHORYLATION. Proc Natl Acad Sci U S A. 1963 May;49(5):715–722. doi: 10.1073/pnas.49.5.715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Howell S. H., Moudrianakis E. N. Function of the "quantasome" in photosynthesis: structure and properties of membrane-bound particle active in the dark reactions of photophosphorylation. Proc Natl Acad Sci U S A. 1967 Sep;58(3):1261–1268. doi: 10.1073/pnas.58.3.1261. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Howell S. H., Moudrianakis E. N. Hill reaction site in chloroplast membranes: non-participation of the quantasome particle in photoreduction. J Mol Biol. 1967 Jul 28;27(2):323–333. doi: 10.1016/0022-2836(67)90023-x. [DOI] [PubMed] [Google Scholar]
  6. Karu A. E., Moudrianakis E. N. Fractionation and comparative studies of enzymes in aqueous extracts of spinach chloroplasts. Arch Biochem Biophys. 1969 Feb;129(2):655–671. doi: 10.1016/0003-9861(69)90226-4. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. McCarty R. E., Racker E. Effect of a coupling factor and its antiserum on photophosphorylation and hydrogen ion transport. Brookhaven Symp Biol. 1966;19:202–214. [PubMed] [Google Scholar]
  9. VAMBUTAS V. K., RACKER E. PARTIAL RESOLUTION OF THE ENZYMES CATALYZINE PHOTOPHOSPHORYLATION. I. STIMULATION OF PHOTOPHOSPHORYLATION BY A PREPARATION OF A LATENT, CA++- DEPENDENT ADENOSINE TRIPHOSPHATASE FROM CHLOROPLASTS. J Biol Chem. 1965 Jun;240:2660–2667. [PubMed] [Google Scholar]
  10. Weiss B., Live T. R., Richardson C. C. Enzymatic breakage and joining of deoxyribonucleic acid. V. End group labeling and analysis of deoxyribonucleic acid containing single straned breaks. J Biol Chem. 1968 Sep 10;243(17):4530–4542. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES