Release of oxidized plastocyanin from photosystem I limits electron transfer between photosystem I and cytochrome b6f complex in vivo.

Abstract

We used fast absorbance spectroscopy to investigate in vivo binding dynamics and electron transfer between plastocyanin (pc) and photosystem I (PSI), and cytochrome (cyt) f oxidation kinetics in Chlamydomonas reinhardtii mutants in which either the binding or the release of pc from PSI was diminished. Under single flash-excitation conditions, electron flow between PSI and the cyt complex was not affected by a 5-fold lowering of the binding affinity of pc to PSI, as induced by a mutation replacing the tryptophan-651 of the PsaA subunit by a serine residue (PsaA-W651S). On the other hand, electron flow from PSI to the cyt b(6)f complex was very sensitive to a 2- to 3-fold decrease in the rate of pc release from PSI, obtained by replacing the glutamic acid residue 613 of the PsaB subunit with glutamine (PsaB-E613N). Thus, our data indicate that under these experimental conditions the release of oxidized pc limits electron transfer between cyt b(6)f complex and PSI in vivo.