<?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%">Gonzalez, P. J.</style></author><author><style face="normal" font="default" size="100%">Rivas, M. G.</style></author><author><style face="normal" font="default" size="100%">Brondino, C. D.</style></author><author><style face="normal" font="default" size="100%">Bursakov, S. A.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Inorg Chem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins/antagonists &amp; inhibitors/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio desulfuricans/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Guanine Nucleotides/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Molybdenum/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Nitrate Reductase/antagonists &amp; inhibitors/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Nitrates/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Periplasm/enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Pterins/chemistry</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jul</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=16791644 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">5</style></number><volume><style face="normal" font="default" size="100%">11</style></volume><pages><style face="normal" font="default" size="100%">609-16</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Nitrate reductases are enzymes that catalyze the conversion of nitrate to nitrite. We report here electron paramagnetic resonance (EPR) studies in the periplasmic nitrate reductase isolated from the sulfate-reducing bacteria Desulfovibrio desulfuricans ATCC 27774. This protein, belonging to the dimethyl sulfoxide reductase family of mononuclear Mo-containing enzymes, comprises a single 80-kDa subunit and contains a Mo bis(molybdopterin guanosine dinucleotide) cofactor and a [4Fe-4S] cluster. EPR-monitored redox titrations, carried out with and without nitrate in the potential range from 200 to -500 mV, and EPR studies of the enzyme, in both catalytic and inhibited conditions, reveal distinct types of Mo(V) EPR-active species, which indicates that the Mo site presents high coordination flexibility. These studies show that nitrate modulates the redox properties of the Mo active site, but not those of the [4Fe-4S] center. The possible structures and the role in catalysis of the distinct Mo(V) species detected by EPR are discussed.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">16791644</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0949-8257 (Print)0949-8257 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">REQUIMTE/CQFB, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal.</style></auth-address></record></records></xml>