Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of  Rhodobacter sulfidophilus | Zendy

Tadros Monier H. | Zendy; Hagemann Gesine E. | Zendy; Katsiou Eleni | Zendy; Dierstein Roland | Zendy; Schiltz Emile | Zendy

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Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of Rhodobacter sulfidophilus

Author(s) -

Tadros Monier H.,

Hagemann Gesine E.,

Katsiou Eleni,

Dierstein Roland,

Schiltz Emile

Publication year - 1995

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/0014-5793(95)00645-p

Subject(s) - rhodobacter , bacteriochlorophyll , amino acid , light harvesting complex , pigment , chemistry , molecular mass , peptide sequence , strain (injury) , protein secondary structure , photosynthetic reaction centre , biochemistry , carotenoid , amino acid residue , photosynthesis , stereochemistry , biology , photosystem ii , organic chemistry , mutant , gene , enzyme , anatomy

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.

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