Structural and functional approach toward a classification of the complex cytochrome c system found in sulfate-reducing bacteria.
Following the discovery of the tetraheme cytochrome c3 in the strict anaerobic sulfate-reducing bacteria (Postgate, J.R. (1954) Biochem. J. 59, xi; Ishimoto et al. (1954) Bull. Chem. Soc. Japan 27, 564-565), a variety of c-type cytochromes (and others) have been reported, indicating that the array of heme proteins in these bacteria is complex. We are proposing here a tentative classification of sulfate- (and sulfur-) reducing bacteria cytochromes c based on: number of hemes per monomer, heme axial ligation, heme spin state and primary structures (whole or fragmentary). Different and complementary spectroscopic tools have been used to reveal the structural features of the heme sites.
Moura
J J
JJ
Centro de Tecnologia Química e Biológica, Oeiras, Portugal.
Costa
C
C
Liu
M Y
MY
Moura
I
I
LeGall
J
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D003574:Cytochrome c Group / Q000145:classification*; D003901:Desulfovibrio / Q000201:enzymology*; D006418:Heme / Q000737:chemistry*; D008969:Molecular Sequence Data
D003574:Cytochrome c Group; D006418:Heme; C017165:cytochrome c(3)