@article {6265, title = {Elucidation of the Functional Redox Behavior of Fumarate Reductase from Shewanella frigidimarina by NMR}, journal = {Annals Magnetic Resonance}, volume = {4}, year = {2005}, pages = {24-28}, abstract = {

NMR spectroscopy has been applied with great success to study electron transfer proteins
with multiple redox centers. This study aimed to elucidate the redox behavior the enzyme fumarate
reductase from Shewanella frigidimarina and particularly to reveal the electron transfer mechanism
from the N-terminal domain to the active center. We developed a new strategy encompassing the
acquisition of 1H-EXSY bidimensional spectra for observation of chemical exchange connectivities in
partially oxidized samples of fcc3, estimation of the paramagnetic chemical shifts expected for the
heme substituents and their comparison with NMR spectra obtained in the fully oxidized protein. This
study allowed obtaining the order of oxidation of the different groups (II-I-III, IV) and gave insights of
the functional mechanisms that allow fcc3 to efficiently transfer electrons from the N-terminal domain
to the active center.

}, url = {http://www.auremn.org.br/Annals/2005-vol4-num1/2005-vol4-num1,2-24-28.pdf}, author = {Pessanha, M. and Rothery, E.L. and Louro, R.O. and Turner, D.L. and Miles, C.S. and Reid, G.A. and Chapman, S. K. and Xavier, A. V. and Salgueiro, C.A.} }