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Direct and indirect electron transfer from cytochromes c and c 2 to the photosynthetic reaction center in pigment‐protein complexes isolated from Rhodocyclus gelatinosus
Author(s) -
Matsuura Katsumi,
Fukushima Atsushi,
Shimada Keizo,
Satoh Toshio
Publication year - 1988
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(88)80163-7
Subject(s) - photosynthetic reaction centre , cytochrome , cytochrome c , cytochrome b6f complex , dimer , chemistry , electron transfer , cytochrome c1 , photochemistry , electron transport chain , bacteriochlorophyll , stereochemistry , cytochrome b , coenzyme q – cytochrome c reductase , photosynthesis , biochemistry , photosystem i , organic chemistry , photosystem ii , enzyme , mitochondrion , mitochondrial dna , gene
Electron transfer from soluble cytochromes c and c 2 to the photo‐oxidized bacteriochlorophyll dimer was studied in photosynthetic reaction center (RC) complexes and RC‐B870 complexes isolated from Rhodocyclus gelatinosus . In the RC‐B870 complex which consists of 6 polypeptides including a bound cytochrome subunit, cytochrome c from horse heart or cytochrome c 2 , from R. gelatinosus was oxidized by photo‐oxidized bacteriochlorophyll dimer indirectly via cytochrome c ‐555 in the complex. In the RC complex which is composed of two polypeptides, the oxidized bacteriochlorophyll dimer was reduced directly by the soluble cytochromes. Although direct electron transfer from soluble cytochrome does not function in R. gelatinosus in vivo, it would replace indirect electron donation if the bound cytochrome were lost mutationally.