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Title: Characteristics and amino-acid composition of a c-type cytochrome in electron acceptor function during thiosulfate-linked photoautotrophic growth of Rhodopseudomonas palustris. Author: Schmitt W, Schleifer G, Horstmann HJ, Knobloch K. Journal: Hoppe Seylers Z Physiol Chem; 1983 Jun; 364(6):647-50. PubMed ID: 6309643. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]