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Antenna holochrome B880 of Rhodospirillum rubrum S1. Pigment, phospholipid, and polypeptide composition

AuthorsPicorel Castaño, Rafael ; Bélanger, Gilles; Gingras, Gabriel
Issue Date1983
PublisherAmerican Chemical Society
CitationBiochemistry 22 (10): 2491-2497 (1983)
AbstractAn antenna bacteriochlorophyll-protein complex (holochrome B880) was isolated from chromatophores of Rhodospirillum rubrum. The yield of chromatophore bacteriochlorophyll recovered as holochrome was about 90% in the initial crude fractions and about 75% after two chromatographic purification steps. The holochrome protein is estimated to account for approximately 60% of the total chromatophore proteins. According to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, this preparation contains two different polypeptides, designated α and β, of apparent Mr 7600 and 6400. Very likely, polypeptide α is the organic solvent soluble polypeptide earlier isolated and sequenced in other laboratories. According to their relative intensity of staining by Coomassie Brilliant Blue in polyacrylamide gels, polypeptides α and β are present in an equimolar ratio. Amino acid analysis of the holochrome and of the polypeptides α and β prepared from it shows the two polypeptides to have different amino acid compositions and agrees with a 1:1 mole ratio. Bacteriochlorophyll and spirilloxanthin, the pigments of the holochrome, are present in a 2:1 mole ratio. The-minimal mass of protein (minimal molecular weight) associated with 2 mol of bacteriochlorophyll and 1 mol of spirilloxanthin is 23000. The data indicate that the minimal oligomer has an α2β2 structure. The holochrome preparation contains about 10% each of pigments and of phospholipids per unit weight of protein. These phospholipids are phosphatidylethanolamine, phosphatidylglycerol, and diphosphatidylglycerol; they are present in approximate mole ratios of 1.0, 0.5, and 0.5, respectively, per 23000 g of protein.
Publisher version (URL)http://dx.doi.org/10.1021/bi00279a028
Identifiersissn: 0006-2960
Appears in Collections:(EEAD) Artículos
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