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J. Biol. Chem., Vol. 280, Issue 41, 34599-34608, October 14, 2005

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Redox and Spectroscopic Properties of the Escherichia coli Nitric Oxide-detoxifying System Involving Flavorubredoxin and Its NADH-oxidizing Redox Partner^*

From the Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, Apt. 127, 2781-901 Oeiras, Portugal

Under anaerobic conditions, the flavodiiron NO-reductase from Escherichia coli (flavorubredoxin, FlRd) constitutes one of the major protective enzymes against nitric oxide. The redox and spectroscopic properties of the rubredoxin (Rd), non-heme diiron, and FMN sites of flavorubredoxin were determined, which was complemented by the study of truncated versions of FlRd: one consisting only of its rubredoxin module, and another consisting of its flavodiiron structural core (lacking the Rd domain). The studies here reported were performed by a combination of potentiometry with visible and EPR spectroscopies. Moreover, we present the first direct EPR evidence for the presence of the non-heme diiron site in the flavodiiron proteins family. Also, the redox properties of the FlRd physiological partner, the NADH:flavorubredoxin oxidoreductase (FlRd-Red), were determined. It is further shown that the redox properties of this complex electron transfer system are fine-tuned upon interaction of the two enzymes.

Received for publication, June 10, 2005 , and in revised form, August 1, 2005.

^* This work was supported in part by Fundação para a Ciência e Tecnologia Project Grant POCTI/2002/BME/44597 (to M. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of Fundação para a Ciência e Tecnologia PhD Grant SFRH/BD/9136/2002.

² To whom correspondence should be addressed: Tel.: 351-21-446-9322; Fax: 351-21-446-9314; E-mail: miguel{at}itqb.unl.pt.

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