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Selective photochemical reduction of either of the two bacteriopheophytins in reaction centers of Rps. sphaeroides R‐26
Author(s) -
Robert Bruno,
Lutz Marc,
Tiede David M.
Publication year - 1985
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(85)80803-6
Subject(s) - bacteriochlorophyll , photosynthetic reaction centre , chemistry , photochemistry , rhodobacter sphaeroides , redox , electron transfer , photosynthesis , acceptor , electron acceptor , electron transport chain , molecule , biochemistry , inorganic chemistry , physics , organic chemistry , condensed matter physics
The bacterial photosynthetic reaction center (RC) contains two bacteriopheophytin (BPh) molecules, only one of which (characterized by Q x,y maxima at 540 and 760 nm) has been found to function in the normal photochemistry. We present here the formation of a new RC redox state, in which the apparently inactive BPh (Q x,y maxima at 530 and 752 nm) is selectively trapped in a reduced state by secondary photochemistry. This BPh is found to be associated to a bacteriochlorophyll (BChI), forming a BChl‐BPh complex analogous to the photochemically active BChl‐BPh acceptor complex. Electron transfer between the two BPhs is found not to occur.