Characteristics and amino-acid composition of a c-type cytochrome in electron acceptor function during thiosulfate-linked photoautotrophic growth of Rhodopseudomonas palustris.
The purple bacterium Rhodopseudomonas palustris (Rhodospirillaceae) was grown in the light with thiosulfatee as the only electron source and HCO theta 3/CO2 as carbon requirement. During thiosulfat oxidation, photolithoautotrophically growing cells transferred the electrons enzymatically towards an endogenous, soluble cytochrome of type c. The cytochrome c in electron acceptor function was purified to homogeneity and appeared as a single protein band in a dodecyl sulfate disc gel electrophoresis. Its molecular mass was determined to be about 16000 Da and its pI value 10.0. The determination of its amino-acid composition revealed a long-chained cytochrome represented by more than 120 amino-acid residues with a characteristic content of lysine and a lack of tryptophan.
D000596:Amino Acids / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D003574:Cytochrome c Group / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D012241:Rhodopseudomonas / Q000201:enzymology* / Q000254:growth & development; D013885:Thiosulfates / Q000378:metabolism*
D000596:Amino Acids; D003574:Cytochrome c Group; D013885:Thiosulfates