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Kinetics of electron transfer in reaction center‐cytochrome o proteoliposomes
Author(s) -
Moser Christopher C.,
Matsushita Kazunobu,
Robertson Dan E.,
Kaback H.Ronald,
Leslie Dutton P.
Publication year - 1986
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(86)80061-8
Subject(s) - photosynthetic reaction centre , chemistry , rhodobacter sphaeroides , redox , kinetics , electron transfer , cytochrome , electron transport chain , photochemistry , cyanide , cytochrome c , heme , flash photolysis , stereochemistry , photosynthesis , reaction rate constant , biochemistry , inorganic chemistry , enzyme , mitochondrion , physics , quantum mechanics
A proteoliposome hybrid protein system consisting of photosynthetic reaction centers (RC) from Rhodopseudomonas sphaeroides , cytochrome o from E. coli and ubiquinone‐8 has been reconstituted to study the mechanism of O 2 reduction and the generation of Δs̃mH + in cyt. o . Steady‐state illumination leads to O 2 uptake and the generation of an interior negative ΔΨ. A rapid flash of light induces a single turnover of each RC, and the resultant pulse of quinol leads to quinonoid inhibitor‐sensitive millisecond reduction kinetics and cyanide‐sensitive re‐oxidation kinetics of cyt o . The b hemes are similar on a kinetic, redox and α‐band spectral basis.