@article {2601,
	title = {Characterization of the cytochrome system of a nitrogen-fixing strain of a sulfate-reducing bacterium: Desulfovibrio desulfuricans strain Berre-Eau},
	journal = {Eur J Biochem},
	volume = {162},
	number = {3},
	year = {1987},
	note = {<p>0014-2956 (Print)0014-2956 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tResearch Support, U.S. Gov{\textquoteright}t, Non-P.H.S.</p>
},
	month = {Feb 2},
	pages = {547-54},
	abstract = {<p>Two c-type cytochromes were purified and characterized by electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopic techniques, from the sulfate-reducer nitrogen-fixing organism, Desulfovibrio desulfuricans strain Berre-Eau (NCIB 8387). The purification procedures included several chromatographic steps on alumina, carboxymethylcellulose and gel filtration. A tetrahaem and a monohaem cytochrome were identified. The multihaem cytochrome has visible, EPR and NMR spectra with general properties similar to other low-potential bis-histidinyl axially bound haem proteins, belonging to the class of tetrahaem cytochrome c3 isolated from other Desulfovibrio species. The monohaem cytochrome c553 is ascorbate-reducible and its EPR and NMR data are characteristic of a cytochrome with methionine-histidine ligation. Their properties are compared with other homologous proteins isolated from sulfate-reducing bacteria.</p>
},
	keywords = {Cytochrome c Group/*analysis, Desulfovibrio/*enzymology, Electron Spin Resonance Spectroscopy, Heme/analysis, Magnetic Resonance Spectroscopy, Molecular Weight, Nitrogen Fixation, Oxidation-Reduction, Spectrophotometry, Sulfates/metabolism, Temperature},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=3030740 },
	author = {Moura, I. and Fauque, G. and Legall, J. and Xavier, A. V. and Moura, J. J.}
}
