Dynamic protein conformations preferentially drive energy transfer along the active chain of the photosystem II reaction centre.

ABSTRACT: One longstanding puzzle concerning photosystem II, a core component of photosynthesis, is that only one of the two symmetric branches in its reaction centre is active in electron transfer. To investigate the effect of the photosystem II environment on the preferential selection of the energy transfer pathway (a prerequisite for electron transfer), we have constructed an exciton model via extensive molecular dynamics simulations and quantum mechanics/molecular mechanics calculations based on a recent X-ray structure. Our results suggest that it is essential to take into account an ensemble of protein conformations to accurately compute the site energies. We identify the cofactor CLA606 of active chain as the most probable site for the energy excitation. We further pinpoint a number of charg

SUBMITTER: Zhang L 

PROVIDER: S-EPMC4083425 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature