<?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%">Almendra, M. J.</style></author><author><style face="normal" font="default" size="100%">Brondino, C. D.</style></author><author><style face="normal" font="default" size="100%">Gavel, O.</style></author><author><style face="normal" font="default" size="100%">Pereira, A. S.</style></author><author><style face="normal" font="default" size="100%">Tavares, P</style></author><author><style face="normal" font="default" size="100%">Bursakov, S.</style></author><author><style face="normal" font="default" size="100%">Duarte, R.</style></author><author><style face="normal" font="default" size="100%">Caldeira, J.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aerobiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromatography, Gel</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*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%">Formate Dehydrogenases/*chemistry/*isolation &amp; purification/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Guanine Nucleotides/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloproteins/chemistry/isolation &amp; purification/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Weight</style></keyword><keyword><style  face="normal" font="default" size="100%">Pterins/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrophotometry, Ultraviolet</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectroscopy, Mossbauer</style></keyword><keyword><style  face="normal" font="default" size="100%">Tungsten/*chemistry</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Dec 7</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=10587462 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">49</style></number><volume><style face="normal" font="default" size="100%">38</style></volume><pages><style face="normal" font="default" size="100%">16366-72</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;An air-stable formate dehydrogenase (FDH), an enzyme that catalyzes the oxidation of formate to carbon dioxide, was purified from the sulfate reducing organism Desulfovibrio gigas (D. gigas) NCIB 9332. D. gigas FDH is a heterodimeric protein [alpha (92 kDa) and beta (29 kDa) subunits] and contains 7 +/- 1 Fe/protein and 0.9 +/- 0.1 W/protein. Selenium was not detected. The UV/visible absorption spectrum of D. gigas FDH is typical of an iron-sulfur protein. Analysis of pterin nucleotides yielded a content of 1.3 +/- 0.1 guanine monophosphate/mol of enzyme, which suggests a tungsten coordination with two molybdopterin guanine dinucleotide cofactors. Both Mossbauer spectroscopy performed on D. gigas FDH grown in a medium enriched with (57)Fe and EPR studies performed in the native and fully reduced state of the protein confirmed the presence of two [4Fe-4S] clusters. Variable-temperature EPR studies showed the presence of two signals compatible with an atom in a d(1) configuration albeit with an unusual relaxation behavior as compared to the one generally observed for W(V) ions.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">10587462</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0006-2960 (Print)0006-2960 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Departamento de Quimica (Centro de Quimica Fina e Biotecnologia), Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, Portugal.</style></auth-address></record></records></xml>