EPR properties of the reaction center of Rhodopseudomas gelatinosa in situ and in a detergent-solubilized form.
The photochemical reaction centers from a variety of purple photosynthetic bacteria are composed of a trimer of protein subunits. However, the recently isolated reaction center from Rhodopseudomonas gelatinosa appears to have only two subunits. In this paper we examine the EPR characteristics of the primary photochemical reactants in this species, and compare them with those of other species. Despite of the differences in protein composition, no dramatic differences in EPR properties are seen in vivo, although some interesting effects are seen upon solubilization of the reaction center, which may be related to the unusual lability of the isolated preparation. Perhaps the most noteworthy phenomenon seen in Rps. gelatinosa is the apparent ability of electrons on the reduced intermediary electron carrier to tunnel at low temperatures to the oxidized c-type cytochrome, which has not been seen in other species studied to date.
D001426:Bacterial Proteins / Q000378:metabolism; D001429:Bacteriochlorophylls / Q000378:metabolism; D002734:Chlorophyll / Q000031:analogs & derivatives; D003574:Cytochrome c Group / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D008027:Light; D008565:Membrane Proteins; D010788:Photosynthesis; D012241:Rhodopseudomonas / Q000378:metabolism; D012995:Solubility; D013045:Species Specificity
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D003574:Cytochrome c Group; D008565:Membrane Proteins; D002734:Chlorophyll