Abstract
The primary processes in photosynthesis occur in pigment-protein complex called reaction centers. The Chloroflexus aurantiacus (C. aurantiacus) reaction center is the smallest functionally active reaction center which has been isolated so far: it is composed of only two protein subunits, instead of four in Rhodopseudomonas viridis and three in Rhodobacter sphaeroides. As in the reaction centers of purple bacteria, the primary donor P is a dimer of bacteriochlorophyll (Bchl). In contrast, the different pigment composition (3 Bchl:3 Bphe) together with spectroscopic data (1,2), suggest that the accessory Bchl (BM)on the inactive M branch in reaction centers from purple bacteria, has been replaced by a bacteriopheophytin (Bphe) in C. aurantiacus reaction centers.
© 1990 Optical Society of America
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