Thapper A. auteur aut IRD Rivas M.G. auteur aut IRD Brondino C.D. auteur aut IRD Ollivier Bernard auteur aut IRD Fauque Guy auteur aut IRD Moura I. auteur aut IRD Moura J. J. G. auteur aut IRD text journalArticle eng text/pdf born digital access Aldehyde oxidoreductase (AOR) activity has been found in a number of sulfate-reducing bacteria. The enzyme that is responsible for the conversion of aldehydes to carboxylic acids is a mononuclear molybdenum enzyme belonging to the xanthine oxidase family. We report here the purification and characterization of AOR isolated from the sulfate-reducing bacterium Desulfovibrio (D.) aminophilus DSM 12254, an aminolytic strain performing thiosulfate dismutation. The enzyme is a homodimer (ca. 200 kDa), containing a molybdenum centre and two [2Fe-2S] clusters per monomer. UV/Visible and electron paramagnetic resonance (EPR) spectra of D. aminophilus AOR recorded in as-prepared and reduced states are similar to those obtained in AORs from Desulfovibrio gigas, Desulfovibrio desulfuricans and Desulfovibrio alaskensis. Despite AOR from D. aminophilus is closely related to other AORs, it presents lower activity towards aldehydes and no activity towards N-heterocyclic compounds, which suggests another possible role for this enzyme in vivo. A comparison of the molecular and EPR properties of AORs from different Desulfovibrio species is also included. (C) 2005 Elsevier Inc. All rights reserved. specialized aldehyde oxidoreductase Desulfovibrio aminophilus mononuclear molybdenum enzymes xanthine oxidase family sulfate reducing bacteria 084 100 1 44-50 2006 0162-0134 https://www.documentation.ird.fr/hor/fdi:010051885 10.1016/j.jinorgbio.2005.09.013 0162-0134 [F B010051885] https://www.documentation.ird.fr/hor/fdi:010051885 https://www.documentation.ird.fr/intranet/publi/depot/2011-06-01/010051885.pdf Accès réservé (Intranet de l'IRD) IRD - Base Horizon / Pleins textes 2006-03-30 2017-08-23 fdi:010051885 fre