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Modification of protein hydrogen bonds influences the efficiency of picosecond electron transfer in bacterial photosynthetic reaction centers
Author(s) -
Paschenko Vladimir Z.,
Korvatovsky Boris N.,
Logunov Stepan L.,
Konko Alexander A.,
Knox Peter P.,
Zakharova Natalya I.,
Grishanova Nadezhda P.,
Rubin Andrew B.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80007-8
Subject(s) - chemistry , photochemistry , photosynthetic reaction centre , ethylene glycol , electron donor , electron transfer , hydrogen bond , kinetic isotope effect , deuterium , organic chemistry , molecule , physics , quantum mechanics , catalysis
Picosecond absorption spectroscopy was used to monitor laser‐induced oxidation‐reductions of reaction center (RC) bacteriochlorophyll (P) and bacteriopheophytin (I) in Rhodopseudomonas sphaeroides RC preparations on exposure to different chemicals. The D 2 O isotope substitution of H 2 O or partial substitution of water by organic solvents (ethylene glycol, glycerol, propylene glycol, dimethyl sulfoxide) causes the appearance of a fast, nanosecond component of P + reduction, the result of an increased probability of recombination of the primary ion‐radical products P + I − → PI. The effect is accompanied by a noticeable slowing down of electron transfer from photoreduced bacteriopheophytin to the primary quinone acceptor Q A . The effect of the organic solvents, known as cryoprotectors, is correlated with their degree of hydrophobicity, i.e. the ability to penetrate the RC protein and interact with bound water and protein hydrogen bonds. The conclusion drawn from the data is that the dielectric relaxation processes through which the intermediate energy levels of the carriers in the PIQ A system are lowered to levels necessary for the stabilization of the photochemically separated charges proceed with the involvement of protons of the nearest water‐protein surrounding of the RC pigments and electron transport cofactors.