Nuclear-magnetic-resonance studies of Desulfuromonas acetoxidans cytochrome c551.5 (c7).
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.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003574:Cytochrome c Group; D006089:Gram-Negative Anaerobic Bacteria / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D013696:Temperature
D001426:Bacterial Proteins; D003574:Cytochrome c Group; C017167:cytochrome C(551)