<?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%">Pettigrew, G. W.</style></author><author><style face="normal" font="default" size="100%">Prazeres, S.</style></author><author><style face="normal" font="default" size="100%">Costa, C.</style></author><author><style face="normal" font="default" size="100%">Palma, N.</style></author><author><style face="normal" font="default" size="100%">Krippahl, L.</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%">The structure of an electron transfer complex containing a cytochrome c and a peroxidase</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytochrome c Group/*chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Horses</style></keyword><keyword><style  face="normal" font="default" size="100%">Magnetic Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Peroxidases/*chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protons</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%">Apr 16</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=10196231 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">16</style></number><volume><style face="normal" font="default" size="100%">274</style></volume><pages><style face="normal" font="default" size="100%">11383-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Efficient biological electron transfer may require a fluid association of redox partners. Two noncrystallographic methods (a new molecular docking program and 1H NMR spectroscopy) have been used to study the electron transfer complex formed between the cytochrome c peroxidase (CCP) of Paracoccus denitrificans and cytochromes c. For the natural redox partner, cytochrome c550, the results are consistent with a complex in which the heme of a single cytochrome lies above the exposed electron-transferring heme of the peroxidase. In contrast, two molecules of the nonphysiological but kinetically competent horse cytochrome bind between the two hemes of the peroxidase. These dramatically different patterns are consistent with a redox active surface on the peroxidase that may accommodate more than one cytochrome and allow lateral mobility.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">10196231</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0021-9258 (Print)0021-9258 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Department of Preclinical Veterinary studies, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Summerhall Edinburgh EH9 1QH, United Kingdom. graham@lab0.vet.ed.ac.uk</style></auth-address></record></records></xml>