A protein dynamics study of photosystem II: the effects of protein conformation on reaction center function.

ABSTRACT: Molecular dynamics simulations have been performed to study photosystem II structure and function. Structural information obtained from simulations was combined with ab initio computations of chromophore excited states. In contrast to calculations based on the x-ray structure, the molecular-dynamics-based calculations accurately predicted the experimental absorbance spectrum. In addition, our calculations correctly assigned the energy levels of reaction-center (RC) chromophores, as well as the lowest-energy antenna chlorophyll. The primary and secondary quinone electron acceptors, Q(A) and Q(B), exhibited independent changes in position over the duration of the simulation. Q(B) fluctuated between two binding sites similar to the proximal and distal sites previously observed in light- and d

SUBMITTER: Vasil'ev S 

PROVIDER: S-EPMC1432123 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature