Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of Rhodobacter sulfidophilus
- 17 July 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 368 (2) , 243-247
- https://doi.org/10.1016/0014-5793(95)00645-p
Abstract
The peripheral light-harvesting bacteriochlorophyll-carotenoid-protein complex B800-850 (LHII) has been isolated from membranes of semi-aerobic dark-grown cells of Rhodobacter sulfidophilus strain W4. A reversed-phase HPLC system resolved one β- and one α-polypeptide in the ratio 1:1. The material obtained was of high purity and suitable for direct microsequence analysis. The primary structures of the β- and α-polypeptides have been determined. The β-polypeptide consists of 51 amino acid residues, yielding a molecular mass of 5512 Da and having 64.7% hydrophobicity. The α-polypeptide consists of 52 amino acid residues, with a calculated molecular mass of 5661 Da and 75% hydrophobicity. The significance of uncommon structure motives with respect to the unusual spectroscopic characteristics of this light-harvesting complex is discussed.Keywords
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