title: The primary structure of the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveals an unusual type of diheme cytochrome c.
abstract: The complete amino acid sequence of the unusual diheme split-Soret cytochrome c from the sulphate-reducing Desulfovibrio desulfuricans strain ATCC 27774 has been determined using classical chemical sequencing techniques and mass spectrometry. The 247-residue sequence shows almost no similarity with any other known diheme cytochrome c, but the heme-binding site of the protein is similar to that of the cytochromes c3 from the sulphate reducers. The cytochrome-c-like domain of the protein covers only the C-terminal part of the molecule, and there is evidence for at least one more domain containing four cysteine residues, which might bind another cofactor, possibly a non-heme iron-containing cluster. This domain is similar to a sequence fragment of the genome of Archaeoglobus fulgidus, which confirms the high conservation of the genes involved in sulfate reduction.
authors.affiliation: Department of Biochemistry, Physiology and Microbiology, University of Gent, Belgium.
authors.forename: B
authors.initials: B
authors.lastname: Devreese
authors.forename: C
authors.initials: C
authors.lastname: Costa
authors.forename: H
authors.initials: H
authors.lastname: Demol
authors.forename: V
authors.initials: V
authors.lastname: Papaefthymiou
authors.forename: I
authors.initials: I
authors.lastname: Moura
authors.forename: J J
authors.initials: JJ
authors.lastname: Moura
authors.forename: J
authors.initials: J
authors.lastname: Van Beeumen
mesh_terms: D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry* / Q000145:classification; D003901:Desulfovibrio / Q000201:enzymology*; D006418:Heme / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D015204:Spectroscopy, Mossbauer
chemical_list: D003574:Cytochrome c Group; D006418:Heme