Bacteriochlorin-protein interactions in native B800-B850, B800 deficient and B800-Bchla(p)-reconstituted complexes from Rhodopseudomonas acidophila, strain 10050.
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 Bchla(p), esterified with phytol. We have investigated the bacteriochlorophylla-protein interactions in native, B800 deficient (or B850) and in B8110-bacteriochlorophylla(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.
Gall
A
A
Section de Biophysique des Protéines et des Membranes, DBCM/CEA and URA2096/CNRS, CEA-Saclay, Gif-sur-Yvette, France.
Fraser
N J
NJ
Bellissent-Funel
M C
MC
Scheer
H
H
Robert
B
B
Cogdell
R J
RJ
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls / Q000378:metabolism*; D002338:Carotenoids / Q000378:metabolism; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D012241:Rhodopseudomonas / Q000378:metabolism*
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; C023693:protein complex B800-850, Rhodobacter; D002338:Carotenoids