Dynamics of electron transfer from high-potential cytochrome c to bacteriochlorophyll dimer in photosynthetic reaction centers as probed using laser-induced temperature jump.
Laser-induced temperature jump experiments were used for testing the rates of thermoinduced conformational transitions of reaction center (RC) complexes in chromatophores of Chromatium minutissimum. The thermoinduced transition of the macromolecular RC complex to a state providing effective electron transport from the multiheme cytochrome c to the photoactive bacteriochlorophyll dimer within the temperature range 220-280 K accounts for tens of seconds with activation energy 0.166 eV/molecule. The rate of the thermoinduced transition in the cytochrome-RC complex was found to be three orders of magnitude slower than the rate of similar thermoinduced transition of the electron transfer reaction from the primary to secondary quinone acceptors studied in the preceding work (Chamorovsky et al. in Eur Biophys J 32:537-543, 2003). Parameters of thermoinduced activation of the electron transfer from the multiheme cytochrome c to the photoactive bacteriochlorophyll dimer are discussed in terms of cytochrome c docking onto the RC.
Chamorovsky
Sergei K
SK
Department of Biophysics, Biology Faculty, Lomonosov Moscow State University, 119992, Moscow, Russia. chamorovsky@interwave.ru
Chamorovsky
Constantine S
CS
Knox
Peter P
PP
Chizhov
Igor V
IV
Zubov
Boris V
BV
D001429:Bacteriochlorophylls / Q000502:physiology*; D002844:Chromatium / Q000502:physiology*; D045304:Cytochromes c / Q000502:physiology*; D019281:Dimerization; D004579:Electron Transport; D007834:Lasers; D045322:Photosynthetic Reaction Center Complex Proteins / Q000502:physiology*; D013696:Temperature
D001429:Bacteriochlorophylls; D045322:Photosynthetic Reaction Center Complex Proteins; D045304:Cytochromes c