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Bacteriochlorin‐protein interactions in native B800‐B850, B800 deficient and B800‐Bchl a p ‐reconstituted complexes from Rhodopseudomonas acidophila , strain 10050
Author(s) -
Gall Andrew,
Fraser Niall J.,
Bellissent-Funel Marie-Claire,
Scheer Hugo,
Robert Bruno,
Cogdell Richard J.
Publication year - 1999
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/s0014-5793(99)00410-x
Subject(s) - bacteriochlorophyll , rhodopseudomonas , chemistry , strain (injury) , triad (sociology) , pigment , stereochemistry , photochemistry , biochemistry , biology , organic chemistry , photosynthesis , anatomy , psychology , psychoanalysis
Recently, a method which allows the selective release and removal of the 800 nm absorbing bacteriochlorophyll a (B800) molecules from the LH2 complex of Rhodopseudomonas acidophila strain 10050 has been described [Fraser, N.J. (1999) Ph.D. Thesis, University of Glasgow, UK]. This procedure also allows the reconstitution of empty binding sites with the native pigment Bchl a p , esterified with phytol. We have investigated the bacteriochlorophyll a ‐protein interactions in native, B800 deficient (or B850) and in B800‐bacteriochlorophyll a p ‐reconstituted LH2 complexes by resonance Raman spectroscopy. We present the first direct structural evidence which shows that the reconstituted pigments are correctly bound within their binding pockets.