The influence of hydrogen bonds on electron transfer rate in photosynthetic RCs.
Hydrogen bonds formed between photosynthetic reaction centers (RCs) and their cofactors were shown to affect the efficacy of electron transfer. The mechanism of such influence is determined by sensitivity of hydrogen bonds to electron density rearrangements, which alter hydrogen bonds potential energy surface. Quantum chemistry calculations were carried out on a system consisting of a primary quinone Q(A), non-heme Fe(2+) ion and neighboring residues(.) The primary quinone forms two hydrogen bonds with its environment, one of which was shown to be highly sensitive to the Q(A) state. In the case of the reduced primary quinone two stable hydrogen bond proton positions were shown to exist on [Q(A)-His(M219)] hydrogen bond line, while there is only one stable proton position in the case of the oxidized primary quinone. Taking into account this fact and also the ability of proton to transfer between potential energy wells along a hydrogen bond, theoretical study of temperature dependence of hydrogen bond polarization was carried out. Current theory was successfully applied to interpret dark P(+)/Q(A)(-) recombination rate temperature dependence.
Krasilnikov
P M
PM
Biological faculty, M.V. Lomonosov Moscow State University, 119899 Moscow, Vorob'evy Gory, Russia.
Mamonov
P A
PA
Knox
P P
PP
Paschenko
V Z
VZ
Rubin
A B
AB
D001429:Bacteriochlorophylls / Q000378:metabolism; D019281:Dimerization; D004579:Electron Transport; D006860:Hydrogen Bonding; D008956:Models, Chemical; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics / Q000378:metabolism*; D011522:Protons; D011789:Quantum Theory; D011809:Quinones / Q000378:metabolism; D012242:Rhodobacter sphaeroides / Q000235:genetics / Q000378:metabolism; D013696:Temperature
D001429:Bacteriochlorophylls; D045322:Photosynthetic Reaction Center Complex Proteins; D011522:Protons; D011809:Quinones