<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Teixeira, M.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Fauque, G.</style></author><author><style face="normal" font="default" size="100%">Dervartanian, D. V.</style></author><author><style face="normal" font="default" size="100%">Legall, J.</style></author><author><style face="normal" font="default" size="100%">Peck, H. D., Jr.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Huynh, B. H.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mossbauer characterization</style></title><secondary-title><style face="normal" font="default" size="100%">Eur J Biochem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy/methods</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogenase/isolation &amp; purification/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron-Sulfur Proteins/isolation &amp; purification/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Macromolecular Substances</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloproteins/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Nickel/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Selenium/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrum Analysis/methods</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1990</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Apr 30</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=2159882 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">2</style></number><volume><style face="normal" font="default" size="100%">189</style></volume><pages><style face="normal" font="default" size="100%">381-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">2159882</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0014-2956 (Print)0014-2956 (Linking)Journal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Centro de Quimica Estrutural, Lisboa, Portugal.</style></auth-address></record></records></xml>