@article {2565,
	title = {The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mossbauer characterization},
	journal = {Eur J Biochem},
	volume = {189},
	number = {2},
	year = {1990},
	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.Research Support, U.S. Gov{\textquoteright}t, P.H.S.</p>
},
	month = {Apr 30},
	pages = {381-6},
	abstract = {<p>The soluble (cytoplasmic plus periplasmic) Ni/Fe-S/Se-containing hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified from cells grown in an 57Fe-enriched medium, and its iron-sulfur centers were extensively characterized by Mossbauer and EPR spectroscopies. The data analysis excludes the presence of a [3Fe-4S] center, either in the native (as isolated) or in the hydrogen-reduced states. In the native state, the non-heme iron atoms are arranged as two diamagnetic [4Fe-4S]2+ centers. Upon reduction, these two centers exhibit distinct and unusual Mossbauer spectroscopic parameters. The centers were found to have similar mid-point potentials (approximately -315 mV) as determined by oxidation-reduction titratins followed by EPR.</p>
},
	keywords = {Desulfovibrio/*enzymology, Electron Spin Resonance Spectroscopy/methods, Hydrogenase/isolation \& purification/*metabolism, Iron-Sulfur Proteins/isolation \& purification/*metabolism, Macromolecular Substances, Metalloproteins/*metabolism, Nickel/analysis, Protein Conformation, Selenium/analysis, Spectrum Analysis/methods},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=2159882 },
	author = {Teixeira, M. and Moura, I. and Fauque, G. and Dervartanian, D. V. and Legall, J. and Peck, H. D., Jr. and Moura, J. J. and Huynh, B. H.}
}
