The Primary Structure of the Presumable BChl d-Binding Polypeptide of Chlorobium vibrioforme f. thiosulfatophilum

Abstract
In addition to the previous isolated and sequenced polypeptides from green photosynthetic sulfur bacteria, which are presumably involved in binding BChl c and e, an analogous poly- peptide has been purified from the BChl d-containing bacterium Chlorobium vibrioforme f. thiosulfatophilum. The primary structure of this 6.15 kDa polypeptide was determined. It shows an extremely high homology (98.3%) to the corresponding polypeptide from Pelodictyon luteolum, indicative of an important functional role.

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