Membrane topography of the photosynthetic reaction center polypeptides of Rhodopseudomonas sphaeroides.
作者： Robert C. Bachmann , Kevin Gillies , Jon Y. Takemoto
DOI: 10.1021/BI00519A012
关键词:
摘要: The topography of the photosynthetic reaction center (RC) polypeptides (H, M, and L) was investigated by proteolysis radioiodination membrane vesicles isolated from Rhodopseudomonas sphaeroides. Chromatophores, obtained French-pressed cell lysates, are closed vesicles' oriented inside out with respect to cytoplasmic (cytoplasmic side out). Spheroplast-derived (SDVs), after osmotic lysis lysozyme-treated cells, right in (periplasmic Alpha-Chymotrypsin treatment chromatophores trypsin SDVs resulted cleavage H. did not cleave H, consistently this polypeptide. M L both were apparently affected these proteases. SDV product H identified alpha-chymotryptic (125)I-labeled peptide mapping had a molecular weight 26 000. Membrane surface chloroglycoluril coated on glass tubes preferential labeling chromatophores. radiospecific activities higher as compared Alpha-Chymotryptic maps surface-radioiodinated differed corresponding results indicate asymmetric exposure opposite surfaces R. sphaeroides membrane. Exposed iodination sites more abundant periplasmic than
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