Charge separation, stabilization, and protein relaxation in photosystem II core particles with closed reaction center.

ABSTRACT: The fluorescence kinetics of cyanobacterial photosystem II (PSII) core particles with closed reaction centers (RCs) were studied with picosecond resolution. The data are modeled in terms of electron transfer (ET) and associated protein conformational relaxation processes, resolving four different radical pair (RP) states. The target analyses reveal the importance of protein relaxation steps in the ET chain for the functioning of PSII. We also tested previously published data on cyanobacterial PSII with open RCs using models that involved protein relaxation steps as suggested by our data on closed RCs. The rationale for this reanalysis is that at least one short-lived component could not be described in the previous simpler models. This new analysis supports the involvement of a protein rel

SUBMITTER: Szczepaniak M 

PROVIDER: S-EPMC2716457 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature