An isolated reaction center complex from the green sulfur bacterium Chlorobium vibrioforme can photoreduce ferredoxin at high rates.

Chlorosome-depleted membranes and a reaction center complex with well-defined subunit composition were prepared from the green sulfur bacterium Chlorobium vibrioforme under anaerobic conditions. The reaction center complex contains a 15-kDa polypeptide with the N-terminal amino acid sequence MEPQLSRPETASNQVR/. This sequence is nearly identical to the N-terminus of the pscD gene product from Chlorobium limicola (Hager-Braun et al. (1995) Biochemistry 34: 9617-9624). In the presence of ferredoxin and ferredoxin:NADP(+) oxidoreductase, the membranes and the isolated reaction center complex photoreduced NADP(+) at rates of 333 and 110 μmol (mg bacteriochlorophyll a)(-1) h(-1), respectively. This shows that the isolated reaction center complex contains all the components essential for steady state electron transport. Midpoint potentials at pH 7.0 of 160 mV for cytochrome c 551 and of 245 mV for P840 were determined by redox titration. Antibodies against cytochrome c 551 inhibit NADP(+) reduction while antibodies against the bacteriochlorophyll a-binding Fenna-Matthews-Olson protein do not.