The primary structure of the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveals an unusual type of diheme cytochrome c.
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.
Devreese
B
B
Department of Biochemistry, Physiology and Microbiology, University of Gent, Belgium.
Costa
C
C
Demol
H
H
Papaefthymiou
V
V
Moura
I
I
Moura
J J
JJ
Van Beeumen
J
J
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
D003574:Cytochrome c Group; D006418:Heme