PMID: 9630723Jun 19, 1998Paper

The influence of structural-dynamic organization of RC from purple bacterium rhodobacter sphaeroides on picosecond stages of photoinduced reactions

Biochimica Et Biophysica Acta
V Z PaschenkoA B Rubin

Abstract

Effects of the hydrogen bond network on the rate constants of energy migration (km), charge separation (ke), electron transfer to QA (kQ) and P+I- recombination in RC of Rhodobacter sphaeroides were analysed in control and modified RC preparations at different temperatures. Modification of RC were made by the addition of 40% v/v DMSO. The rate constants km, ke, kQ were evaluated from pump-and-probe measurements of the absorption difference kinetics at 665 nm corresponding to BPhL- formation and subsequent electron transfer to QA. For the investigation of P+I- recombination a primary quinone acceptor was pre-reduced in the dark by adding of 1 mg/ml of dithionite and 1 mM sodium ascorbate. Recombination kinetics were measured at 665 and 870 nm. The numerical analysis of the temperature dependence of ke and kQ was performed on the basis of the model proposed by Kakitani and Kakitani (T. Kakitani and H. Kakitani (1981), Biochim. Biophys. Acta, 635, 498-514). It was found that: (a) in control samples the molecular rate constants km, ke and kQ were about (3.4 ps)-1, (4.5 ps)-1 and (200 ps)-1, respectively; (b) under modification by DMSO these rates decrease up to (5.3 ps)-1, (10.3 ps)-1 and (500 ps)-1, respectively; (c) as the temper...Continue Reading

Citations

Oct 14, 2000·Archives of Biochemistry and Biophysics·J R Tormo, E Estornell
Feb 21, 2008·European Biophysics Journal : EBJ·Adjaci F UchoaMauricio S Baptista
Jun 9, 2016·Nanoscale Research Letters·T V SerdenkoN Kh Seifullina
Apr 20, 2007·Biochimica Et Biophysica Acta·P M KrasilnikovA B Rubin

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