Please use this identifier to cite or link to this item:

Title: Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin
Authors: Broco, Manuela
Soares, Claudio M.
Oliveira, Solange
Mayhew, Stephen G
Rodrigues-Pousada, Claudina
Keywords: Desulfovibrio gigas
Issue Date: 2007
Abstract: Abstract: Flavoredoxin participates in Desulfovibrio gigas thiosulfate reduction pathway. Its 3-dimensional model was generated allowing the oxidized riboflavin-5'-phosphate (FMN) site to be predicted. Residues likely to be involved in FMN-binding were identified (N29, W35, T56, K92, H131 and F164) and mutated to alanine. Fluorescence titration with apoprotein showed that FMN is strongly bound in the wild-type protein. Comparison of K-d values for mutants suggests that interactions with the phosphate group of FMN, contribute more to binding than the interactions with the isoalloxazine ring. The redox potential of bound FMN determined for wild-type and mutants revealed shifts to less negative values. These findings were correlated with the protein structure in order to contribute to a better understanding of the structure-function relationships in flavoredoxin. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Type: article
Appears in Collections:MED - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica
BIO - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica

Files in This Item:

File Description SizeFormat
Molecular determinants for FMN.pdfAbstract35.03 kBAdobe PDFView/Open
FacebookTwitterDeliciousLinkedInDiggGoogle BookmarksMySpaceOrkut
Formato BibTex mendeley Endnote Logotipo do DeGóis 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.


Dspace Dspace
DSpace Software, version 1.6.2 Copyright © 2002-2008 MIT and Hewlett-Packard - Feedback
UEvora B-On Curriculum DeGois