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Volume 272, Number 36, Issue of September 5, 1997 pp. 22502-22508
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Studies on the Redox Centers of the Terminal Oxidase from Desulfovibrio gigas and Evidence for Its Interaction with Rubredoxin

(Received for publication, April 22, 1997, and in revised form, June 30, 1997)

Cláudio M. Gomes , Gabriela Silva ^§ , Solange Oliveira ^§ , Jean LeGall ^¶ , Ming-Yih Liu ^¶ , António V. Xavier , Claudina Rodrigues-Pousada ^§ and Miguel Teixeira

From the  Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal, the ^§ Instituto Gulbenkian de Ciência, Laboratório de Genética Molecular, Oeiras, Portugal, and the ^¶ Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602

Rubredoxin-oxygen oxidoreductase (ROO) is the final component of a soluble electron transfer chain that couples NADH oxidation to oxygen consumption in the anaerobic sulfate reducer Desulfovibrio gigas. It is an 86-kDa homodimeric flavohemeprotein containing two FAD molecules, one mesoheme IX, and one Fe-uroporphyrin I per monomer, capable of fully reducing oxygen to water. EPR studies on the native enzyme reveal two components with g values at ~2.46, 2.29, and 1.89, which are assigned to low spin hemes and are similar to the EPR features of P-450 hemes, suggesting that ROO hemes have a cysteinyl axial ligation. At pH 7.6, the flavin redox transitions occur at 0 ± 15 mV for the quinone/semiquinone couple and at 130 ± 15 mV for the semiquinone/hydroquinone couple; the hemes reduction potential is 350 ± 15 mV. Spectroscopic studies provided unequivocal evidence that the flavins are the electron acceptor centers from rubredoxin, and that their reduction proceed through an anionic semiquinone radical. The reaction with oxygen occurs in the flavin moiety. These data are strongly corroborated by the finding that rubredoxin and ROO are located in the same polycistronic unit of D. gigas genome. For the first time, a clear role for a rubredoxin in a sulfate-reducing bacterium is presented.

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