<?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%">Pessanha, M.</style></author><author><style face="normal" font="default" size="100%">Rothery, E.L.</style></author><author><style face="normal" font="default" size="100%">Louro, R.O.</style></author><author><style face="normal" font="default" size="100%">Turner, D.L.</style></author><author><style face="normal" font="default" size="100%">Miles, C.S.</style></author><author><style face="normal" font="default" size="100%">Reid, G.A.</style></author><author><style face="normal" font="default" size="100%">Chapman, S. K.</style></author><author><style face="normal" font="default" size="100%">Xavier, A. V.</style></author><author><style face="normal" font="default" size="100%">Salgueiro, C.A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Elucidation of the Functional Redox Behavior of Fumarate Reductase from  Shewanella frigidimarina by NMR</style></title><secondary-title><style face="normal" font="default" size="100%">Annals Magnetic Resonance</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2005</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.auremn.org.br/Annals/2005-vol4-num1/2005-vol4-num1,2-24-28.pdf</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">24-28</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;NMR spectroscopy has been applied with great success to study electron transfer proteins&lt;br /&gt;
with multiple redox centers. This study aimed to elucidate the redox behavior the enzyme fumarate&lt;br /&gt;
reductase from Shewanella frigidimarina and particularly to reveal the electron transfer mechanism&lt;br /&gt;
from the N-terminal domain to the active center. We developed a new strategy encompassing the&lt;br /&gt;
acquisition of 1H-EXSY bidimensional spectra for observation of chemical exchange connectivities in&lt;br /&gt;
partially oxidized samples of fcc3, estimation of the paramagnetic chemical shifts expected for the&lt;br /&gt;
heme substituents and their comparison with NMR spectra obtained in the fully oxidized protein. This&lt;br /&gt;
study allowed obtaining the order of oxidation of the different groups (II-I-III, IV) and gave insights of&lt;br /&gt;
the functional mechanisms that allow fcc3 to efficiently transfer electrons from the N-terminal domain&lt;br /&gt;
to the active center. &lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1/2</style></issue></record></records></xml>