Effect of protein relaxation on electron transfer from the cytochrome subunit to the bacteriochlorophyll dimer in Rps. sulfoviridis reaction centers within mixed adiabatic/nonadiabatic model.
The broad set of nonexponential electron transfer (ET) kinetics in reaction centers (RC) from Rhodopseudomonas sulfoviridis in temperature range 297-40 K are described within a mixed adiabatic/nonadiabatic model. The key point of the model is the combination of Sumi-Marcus and Rips-Jortner approaches which can be represented by the separate contributions of temperature-independent vibrational (v) and temperature-dependent diffusive (d) coordinates to the preexponential factor, to the free energy of reaction DeltaG=DeltaG(v)+DeltaG(d)(T) and to the reorganization energy lambda=lambda(v)+lambda(d)(T). The broad distribution of protein dielectric relaxation times along the diffusive coordinate is considered within the Davidson-Cole formalism.
Kotelnikov
A I
AI
Institute of Problems of Chemical Physics RAS, Chernogolovka, 142432 Moscow region, Russia. kotel@icp.ac.ru
Ortega
J M
JM
Medvedev
E S
ES
Psikha
B L
BL
Garcia
D
D
Mathis
P
P
D001426:Bacterial Proteins / Q000737:chemistry*; D001429:Bacteriochlorophylls / Q000737:chemistry*; D003580:Cytochromes / Q000737:chemistry*; D019281:Dimerization; D007700:Kinetics; D008956:Models, Chemical; D012241:Rhodopseudomonas / Q000737:chemistry*; D013816:Thermodynamics
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D003580:Cytochromes