Nov 2, 1984

Nuclear-magnetic-resonance studies of Desulfuromonas acetoxidans cytochrome c551.5 (c7)

European Journal of Biochemistry
J J MouraA V Xavier


1H nuclear magnetic resonance (NMR) spectroscopy has been used to examine cytochrome c551.5 (c7) from the sulfur reducer, Desulfuromonas acetoxidans. This protein contains three hemes. Two stable oxidation states (the fully oxidized and the fully reduced) as well as intermediate oxidation states were studied. The axial ligands of the iron were found to be neutral histidines. The redox properties of cytochrome c7 were examined and good quantitative agreement found between the NMR results and previously reported redox potential measurements. The properties of cytochrome c7 are discussed together with those of the homologous tetraheme cytochromes c3 isolate from sulfate-reducing bacteria.

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Mentioned in this Paper

In Vivo NMR Spectroscopy
Bacterial Proteins
Gram-Negative Anaerobic Bacteria
Cytochrome c Group
Hydrogen-Ion Concentration
CccB protein, Bacillus subtilis

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