The structural organization of the antenna chromophore protein complexes in membranes of the photosynthetic bacterium Rhodopseudomonas viridis.

A possible structural and functional organization of the antenna chromophore protein complexes (CPC) in the Rhodopseudomonas viridis membranes was considered in terms of structural models proposed by Zuber and Brunisholz (in Chlorophylls, ed. H. Scheer (Boca Raton: CRC Press, 1991):626-703). Analysis of the absorption spectra led to the conclusion that the number of the antenna bacteriochlorophyll molecules per reaction center (RC) is 30 +/- 3 both for chromophores and quantasomes of Rps. viridis. It implies a multicentral organization of the CPCs around RCs, when the CPC of cyclic structure is formed by (alpha beta gamma)4 polypeptides. A multicentral model predicts an almost linear dependence of the antenna fluorescence yield on the oxidized primary donor concentration if the antenna fluorescence lifetimes are assumed to be 60-70 and 110-120 ps for the open and closed RCs, respectively, which is in agreement with the experimental observations. We conclude that the Rps. viridis membrane domain consists of 4-6 RCs surrounded by 6-22 CPCs, and both of these protein subsystems are packed into a hexagonal array.