@article {2555,
	title = {Partial purification and characterization of the first hydrogenase isolated from a thermophilic sulfate-reducing bacterium},
	journal = {Biochem Biophys Res Commun},
	volume = {184},
	number = {3},
	year = {1992},
	note = {<p>0006-291X (Print)0006-291X (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tResearch Support, U.S. Gov{\textquoteright}t, Non-P.H.S.</p>
},
	month = {May 15},
	pages = {1256-60},
	abstract = {<p>A soluble [NiFe] hydrogenase has been partially purified from the obligate thermophilic sulfate-reducing bacterium Thermodesulfobacterium mobile. A 17\% purification yield was obtained after four chromatographic steps and the hydrogenase presents a purity index (A398 nm/A277 nm) equal to 0.21. This protein appears to be 75\% pure on SDS-gel electrophoresis showing two major bands of molecular mass around 55 and 15 kDa. This hydrogenase contains 0.6-0.7 nickel atom and 7-8 iron atoms per mole of enzyme and has a specific activity of 783 in the hydrogen uptake reaction, of 231 in the hydrogen production assay and of 84 in the deuterium-proton exchange reaction. The H2/HD ratio is lower than one in the D2-H+ exchange reaction. The enzyme is very sensitive to NO, relatively little inhibited by CO but unaffected by NO2-. The EPR spectrum of the native hydrogenase shows the presence of a [3Fe-4S] oxidized cluster and of a Ni(III) species.</p>
},
	keywords = {Chromatography, Gel, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Desulfovibrio/*enzymology, Electron Spin Resonance Spectroscopy, Hot Temperature, Hydrogenase/*isolation \& purification/*metabolism, Kinetics, Thermodynamics},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=1317168 },
	author = {Fauque, G. and Czechowski, M. and Berlier, Y. M. and Lespinat, P. A. and Legall, J. and Moura, J. J.}
}
