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Title: Transverse topography of the photochemical reaction center polypeptides in the Rhodopseudomonas capsulata membrane

Journal Article · · J. Bacteriol.; (United States)
OSTI ID:6004295

The exposure of the three polypeptide subunits H, M, and L of the photochemical reaction center (RC) on both surfaces of the membrane of Rhodopseudomonas capsulata was studied by partial proteolysis with proteinase K and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of degradation products. The possible association of RC subunits with bacteriochlorophyll a and bacteriopheophytin was investigated by spectroscopical measurements. Chromatophores (inside-out oriented) and spheroplasts (right-side-out oriented), as well as purified, detergent-solubilized RCs and RCs reconstituted into phosphatidyl choline liposomes, were used. Subunit H of the RC was degraded to fragments with apparent M/sub r/s of 15,000 and 12,500 which were possibly derived from cleavage of a loop exposed on the cytoplasmic surface. Polypeptide M was digested at a comparable rate. The apparent M/sub r/ of M decreased by roughly 4000 upon proteolytic cleavage. Subunit L was relatively insensitive to protease attach, except that a small peptide was clipped off. The primary donor P870 was also found to be only slightly affected by proteinase K. All three RC subnunits appear to be exposed on the chromatophore surface.

Research Organization:
Albert-Ludwigs-Univ., Freiburg, West Germany
OSTI ID:
6004295
Journal Information:
J. Bacteriol.; (United States), Vol. 158:3
Country of Publication:
United States
Language:
English