<?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%">de Sousa, P. M.</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Goncalves, M. L.</style></author><author><style face="normal" font="default" size="100%">Pettigrew, G. W.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Dos Santos, M. M.</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%">Mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by P. pantotrophus pseudoazurin: kinetics of intermolecular electron transfer</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%">Azurin/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytochrome-c Peroxidase/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrochemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrodes</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrolytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Transport/*physiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen Peroxide/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Indicators and Reagents</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Paracoccus pantotrophus/*enzymology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jun</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=17361419 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">5</style></number><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">691-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;This work reports the direct electrochemistry of Paracoccus pantotrophus pseudoazurin and the mediated catalysis of cytochrome c peroxidase from the same organism. The voltammetric behaviour was examined at a gold membrane electrode, and the studies were performed in the presence of calcium to enable the peroxidase activation. A formal reduction potential, E (0)', of 230 +/- 5 mV was determined for pseudoazurin at pH 7.0. Its voltammetric signal presented a pH dependence, defined by pK values of 6.5 and 10.5 in the oxidised state and 7.2 in the reduced state, and was constant up to 1 M NaCl. This small copper protein was shown to be competent as an electron donor to cytochrome c peroxidase and the kinetics of intermolecular electron transfer was analysed. A second-order rate constant of 1.4 +/- 0.2 x 10(5) M(-1) s(-1) was determined at 0 M NaCl. This parameter has a maximum at 0.3 M NaCl and is pH-independent between pH 5 and 9.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">17361419</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, Centro de Quimica Fina e Biotecnologia, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.</style></auth-address></record></records></xml>