A new possible binding site for bacteriochlorophyll b in a light‐harvesting polypeptide of the bacterium Ectothiorhodospira halochloris

FEBS Letters

Zuber, Herbert¹  Frank, Gerhard¹  Wagner-Huber, Regula¹  Bissig, Iwan¹  Brunisholz, René A.¹ 

[1] Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, 8093 Zürich, Switzerland

关键词: Purple bacteria;    Bacteriochlorophyll b;    Light-harvesting polypeptide;    Amino acid sequence;    (Ectothiorhodospira halochloris);    LHP;    light-harvesting polypeptide;    Bchl;    bacteriochlorophyll;    PTH;    phenylthiohydantoin;    RP;    reverse phase;    DTT;    1;    4-dithio-DL-threitol;   

DOI  :  10.1016/0014-5793(88)81345-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Whole cells from Ectothiorhodospira halochloris were extracted with an organic solvent mixture. At least five small hydrophobic polypeptides representing most probably the light harvesting polypeptides were purified by gel filtration and consecutive FPLC-RP chromatography. The complete amino acid sequence of a 7.4 kDa polypeptide was determined. The polypeptide shows a three domain structure, indicative of an integral membrane protein, similar to the structure of the light-harvesting polypeptides from purple non-sulfur bacteria. Sequence homologies to the β-LHPs of purple bacteria range from 23. 1° to 36.4°. The conserved intramembrane located histidine residue of the antenna polypeptides of purple non-sulfur bacteria, assigned as the possible binding site for bacteriochlorophyll, was found to be replaced by asparagine.

【 授权许可】

Unknown