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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 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 MrS 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 Mr of M decreased by roughly 4,000 upon proteolytic cleavage. Subunit L was relatively insensitive to protease attack, except that a small peptide was clipped off. The primary donor P870 was also found to be only slightly affected proteinase K. All three RC subunits appear to be exposed on the chromatophore surface.

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