<?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%">Rivas, M. G.</style></author><author><style face="normal" font="default" size="100%">Mota, C. S.</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Carepo, M. S.</style></author><author><style face="normal" font="default" size="100%">Folgosa, F.</style></author><author><style face="normal" font="default" size="100%">Andrade, S. L.</style></author><author><style face="normal" font="default" size="100%">Fauque, G.</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%">Calvete, J. J.</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%">Isolation and characterization of a new Cu-Fe protein from Desulfovibrio aminophilus DSM12254</style></title><secondary-title><style face="normal" font="default" size="100%">J Inorg Biochem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Copper</style></keyword><keyword><style  face="normal" font="default" size="100%">*Iron</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins/*chemistry/genetics/*isolation &amp;</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*chemistry/genetics/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug Resistance, Bacterial/drug effects/physiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloproteins/*chemistry/genetics/*isolation &amp; purification/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Molybdenum/chemistry/pharmacology</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Quaternary/physiology</style></keyword><keyword><style  face="normal" font="default" size="100%">purification/metabolism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Oct</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=19699535 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">10</style></number><volume><style face="normal" font="default" size="100%">103</style></volume><pages><style face="normal" font="default" size="100%">1314-22</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 isolation and characterization of a new metalloprotein containing Cu and Fe atoms is reported. The as-isolated Cu-Fe protein shows an UV-visible spectrum with absorption bands at 320 nm, 409 nm and 615 nm. Molecular mass of the native protein along with denaturating electrophoresis and mass spectrometry data show that this protein is a multimer consisting of 14+/-1 subunits of 15254.3+/-7.6 Da. Mossbauer spectroscopy data of the as-isolated Cu-Fe protein is consistent with the presence of [2Fe-2S](2+) centers. Data interpretation of the dithionite reduced protein suggest that the metallic cluster could be constituted by two ferromagnetically coupled [2Fe-2S](+) spin delocalized pairs. The biochemical properties of the Cu-Fe protein are similar to the recently reported molybdenum resistance associated protein from Desulfovibrio, D. alaskensis. Furthermore, a BLAST search from the DNA deduced amino acid sequence shows that the Cu-Fe protein has homology with proteins annotated as zinc resistance associated proteins from Desulfovibrio, D. alaskensis, D. vulgaris Hildenborough, D. piger ATCC 29098. These facts suggest a possible role of the Cu-Fe protein in metal tolerance.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">19699535</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;1873-3344 (Electronic)0162-0134 (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>