Isolation and characterization of the polypeptide components from light-harvesting pigment-protein complex B800--850 of Rhodopseudomonas capsulata.

The light-harvesting bacteriochlorophyll-carotenoid-protein complex B800--850 has been isolated from membranes of the phototroph-negative mutant strain Y5 of Rhodopseudomonas capsulata. The three polypeptides of the complex have been found to be soluble in chloroform-methanol (1:1, v/v) in the presence of 0.1 M ammonium acetate. They were extracted from the complex and separated by gel filtration on Sephadex LH-60 in the same solvent mixture. Minimum molecular weights based on amino acid composition are 12 000, 9300, and 5100. Values previously determined by sodium dodecyl sulfate/polyacrylamide gel electrophoresis are 14 000, 10 000 and 8000. The two smaller polypeptides (polarities 31% and 39%) are completely soluble in chloroform/methanol/ammonium acetate while the largest and most polar (41%) polypeptide is only partially soluble. The largest polypeptide contains no tryptophan. The middle polypeptide contains no cysteine and arginine, while the small polypeptide lacks cysteine. Methionine is shown to be the amino terminus for the small and middle polypeptides by two independent methods (Edman degradation and dansylation). Both methods also indicated that the N terminus of the 14 000 polypeptide seems to be blocked. Partial N-terminal amino acid sequences were obtained for the two smaller polypeptides. No homology between the two proteins was observed.