Pigment-protein complexes from Rhodopseudomonas palustris: isolation, characterization, and reconstitution into liposomes.

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We have employed detergent solubilization and sucrose density gradient centrifugation to obtain pigment-protein complexes from Rhodopseudomonas palustris. Two types of detergent buffers were used, containing either octyl-beta-glucopyranoside (OG) plus sodium dodecyl sulfate (SDS) or OG alone. The fractions thus obtained were analyzed spectrophotometrically and by polyacrylamide gel electrophoresis to determine their pigment and protein composition. OG-SDS solubilization yields four fractions. The least dense of these fractions (OG-SDS a and b) are nonspecific mixtures of peptides and pigments. The next fraction, OG-SDS c, is an accessory light-harvesting complex, LHII, called B800-850. The largest particle, OG-SDS d, is a combination of reaction center (RC) and primary light-harvesting complex (LHI), B880. Solubilization using OG alone yields one fraction, a single large complex consisting of RC, LHI, and LHII. We have inserted the two large OG-SDS complexes and the OG complex into phospholipid liposomes to determine the size of such complexes in freeze-fractured membranes. On the basis of morphological, biochemical, and available biophysical data, we propose the following models for pigment-protein complexes in R. palustris membranes: 5-nm particles as free RC or LHI tetramers, 7.5-nm particles as LHI or LHII octamers (or both); 10-nm particles as RC-LHI core complexes (1 RC plus 12 LHI) or large LHII oligomers (or both), and large particles of 12.5 and 15 nm and LHII associated with the RC-LHI core complex.

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