Structural, dynamic, and energetic aspects of long-range electron transfer in photosynthetic reaction centers.

ABSTRACT: Intramolecular electron transfer within proteins plays an essential role in biological energy transduction. Electron donor and acceptor cofactors are bound in the protein matrix at specific locations, and protein-cofactor interactions as well as protein conformational changes can markedly influence the electron transfer rates. To assess these effects, we have investigated charge recombination from the primary quinone acceptor to the special pair bacteriochlorophyll dimer in wild-type reaction centers of Rhodobacter sphaeroides and four mutants with widely modified free energy gaps. After light-induced charge separation, the recombination kinetics were measured in the light- and dark-adapted forms of the protein from 10 to 300 K. The data were analyzed by using the spin-boson model, which a

SUBMITTER: Kriegl JM 

PROVIDER: S-EPMC314149 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature