The reaction center (RC) from the photosynthetic bacterium Rhodobacter
(Rb.) capsulatus has been the subject of a considerable amount of mol
ecular biological and spectroscopic work aimed at improving our unders
tanding of the primary steps of photosynthesis. However, no three-dime
nsional structure is available for this protein. We present here a mod
el obtained by combining information from the structure of the highly
homologous RC from Rhodopseudomonas (Rps.) viridis with molecular mech
anics and simulated annealing calculations. In the Rb. capsulatus mode
l the orientations of the bacteriochlorophyll monomer and the bacterio
pheophytin on the branch inactive in electron transfer differ signific
antly from those in the RCs of Rps. viridis and Rb. sphaeroides. The b
acteriopheophytin orientational difference is in good accord with prev
ious linear dichroism measurements. A comparison is made of interactio
ns between the pigments and the protein environment that may be of fun
ctional significance in Rps. viridis, Rb. sphaeroides, and Rb, capsula
tus. (C) 1995 Wiley-Liss, Inc.