Asymmetric electron transfer in cyanobacterial Photosystem I: charge separation and secondary electron transfer dynamics of mutations near the primary electron acceptor A0.
Point mutations were introduced near the primary electron acceptor sites assigned to A0 in both the PsaA and PsaB branches of Photosystem I in the cyanobacterium Synechocystis sp. PCC 6803. The residues Met688PsaA and Met668PsaB, which provide the axial ligands to the Mg2+ of the eC-A3 and eC-B3 chlorophylls, were changed to leucine and asparagine (chlorophyll notation follows Jordan et al., 2001). The removal of the ligand is expected to alter the midpoint potential of the A0/A0- redox pair and result in a change in the intrinsic charge separation rate and secondary electron transfer kinetics from A0- to A1. The dynamics of primary charge separation and secondary electron transfer were studied at 690 nm and 390 nm in these mutants by ultrafast optical pump-probe spectroscopy. The data reveal that mutations in the PsaB branch do not alter electron transfer dynamics, whereas mutations in the PsaA branch have a distinct effect on electron transfer, slowing down both the primary charge separation and the secondary electron transfer step (the latter by a factor of 3-10). These results suggest that electron transfer in cyanobacterial Photosystem I is asymmetric and occurs primarily along the PsaA branch of cofactors.
Dashdorj
Naranbaatar
N
Department of Physics, Purdue University, West Lafayette, Indiana.
Xu
Wu
W
Cohen
Rachel O
RO
Golbeck
John H
JH
Savikhin
Sergei
S
D019943:Amino Acid Substitution; D004579:Electron Transport / Q000528:radiation effects; D007700:Kinetics; D008027:Light; D016297:Mutagenesis, Site-Directed; D045331:Photosystem I Protein Complex / Q000032:analysis / Q000737:chemistry* / Q000528:radiation effects*; D013056:Spectrophotometry, Ultraviolet; D055672:Static Electricity; D013329:Structure-Activity Relationship
D045331:Photosystem I Protein Complex