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. 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.

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Selected References

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

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