Relationship between the oxidation potential of the bacteriochlorophyll dimer and electron transfer in photosynthetic reaction centers.
The primary electron donor in the photosynthetic reaction center from purple bacteria is a bacteriochlorophyll dimer containing four conjugated carbonyl groups that may form hydrogen bonds with amino acid residues. Spectroscopic analyses of a set of mutant reaction centers confirm that hydrogen bonds can be formed between each of these carbonyl groups and histidine residues in the reaction center subunits. The addition of each hydrogen bond is correlated with an increase in the oxidation potential of the dimer, resulting in a 355-mV range in the midpoint potential. The resulting changes in the free-energy differences for several reactions involving the dimer are related to the electron transfer rates using the Marcus theory. These reactions include electron transfer from cytochrome c2 to the oxidized dimer, charge recombination from the primary electron acceptor quinone, and the initial forward electron transfer.
Allen
J P
JP
Department of Chemistry and Biochemistry, State University, Tempe, Arizona 85287-1604, USA.
Williams
J C
JC
D001429:Bacteriochlorophylls / Q000737:chemistry* / Q000378:metabolism*; D004579:Electron Transport; D006860:Hydrogen Bonding; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D008962:Models, Theoretical; D008968:Molecular Conformation; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D017354:Point Mutation; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins