<?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%">Ana C. Messias</style></author><author><style face="normal" font="default" size="100%">António P. Aguiar</style></author><author><style face="normal" font="default" size="100%">Brennan, Lorraine</style></author><author><style face="normal" font="default" size="100%">Salgueiro, C.A.</style></author><author><style face="normal" font="default" size="100%">Saraiva, Lígia M.</style></author><author><style face="normal" font="default" size="100%">Xavier, António V.</style></author><author><style face="normal" font="default" size="100%">Turner, David L.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica et Biophysica Acta (BBA) - Bioenergetics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2006</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.sciencedirect.com/science/article/pii/S000527280600020X</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">1757</style></volume><pages><style face="normal" font="default" size="100%">143-153</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem–haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.&lt;/p&gt;
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