<?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%">Timoteo, C. G.</style></author><author><style face="normal" font="default" size="100%">Guilherme, M.</style></author><author><style face="normal" font="default" size="100%">Penas, D.</style></author><author><style face="normal" font="default" size="100%">Folgosa, F</style></author><author><style face="normal" font="default" size="100%">Tavares, P.</style></author><author><style face="normal" font="default" size="100%">Pereira, AS</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Desulfovibrio vulgaris bacterioferritin uses H(2)O(2) as a co-substrate for iron oxidation and reveals DPS-like DNA protection and binding activities</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem J</style></secondary-title><alt-title><style face="normal" font="default" size="100%">The Biochemical journal</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins/drug effects/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Cloning, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytochrome b Group/drug effects/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio vulgaris/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Bacterial/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA-Binding Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Ferritins/drug effects/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen Peroxide/pharmacology</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidative Stress</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></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Aug 15</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=22642556 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">1</style></number><volume><style face="normal" font="default" size="100%">446</style></volume><pages><style face="normal" font="default" size="100%">125-33</style></pages><isbn><style face="normal" font="default" size="100%">1470-8728 (Electronic)0264-6021 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A gene encoding Bfr (bacterioferritin) was identified and isolated from the genome of Desulfovibrio vulgaris cells, and overexpressed in Escherichia coli. In vitro, H(2)O(2) oxidizes Fe(2+) ions at much higher reaction rates than O(2). The H(2)O(2) oxidation of two Fe(2+) ions was proven by Mossbauer spectroscopy of rapid freeze-quenched samples. On the basis of the Mossbauer parameters of the intermediate species we propose that D. vulgaris Bfr follows a mineralization mechanism similar to the one reported for vertebrate H-type ferritins subunits, in which a diferrous centre at the ferroxidase site is oxidized to diferric intermediate species, that are subsequently translocated into the inner nanocavity. D. vulgaris recombinant Bfr oxidizes and stores up to 600 iron atoms per protein. This Bfr is able to bind DNA and protect it against hydroxyl radical and DNase deleterious effects. The use of H(2)O(2) as an oxidant, combined with the DNA binding and protection activities, seems to indicate a DPS (DNA-binding protein from starved cells)-like role for D. vulgaris Bfr.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">22642556</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;Journal ArticleResearch Support, Non-U.S. Gov'tEngland&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, Quinta da Torre, 2829-516 Caparica, Portugal.</style></auth-address></record></records></xml>