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J Biol Chem, Vol. 274, Issue 51, 36715-36721, December 17, 1999

Identification and Characterization of a Novel Ferric Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus*

Alexander VadasDagger , Harold G. MonbouquetteDagger , Eric Johnson§, and Imke Schröder§

From the Dagger  Department of Chemical Engineering and the § Department of Microbiology and Molecular Genetics, UCLA, Los Angeles, California 90095

Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing Archaeon, contains high Fe3+-EDTA reductase activity in its soluble protein fraction. The corresponding enzyme, which constitutes about 0.75% of the soluble protein, was purified 175-fold to homogeneity. Based on SDS-polyacrylamide gel electrophoresis, the ferric reductase consists of a single subunit with a Mr of 18,000. The Mr of the native enzyme was determined by size exclusion chromatography to be 40,000 suggesting that the native ferric reductase is a homodimer. The enzyme uses both NADH and NADPH as electron donors to reduce Fe3+-EDTA. Other Fe3+ complexes and dichlorophenolindophenol serve as alternative electron acceptors, but uncomplexed Fe3+ is not utilized. The purified enzyme strictly requires FMN or FAD as a catalytic intermediate for Fe3+ reduction. Ferric reductase also reduces FMN and FAD, but not riboflavin, with NAD(P)H which classifies the enzyme as a NAD(P)H:flavin oxidoreductase. The enzyme exhibits a temperature optimum of 88 °C. When incubated at 85 °C, the enzyme activity half-life was 2 h. N-terminal sequence analysis of the purified ferric reductase resulted in the identification of the hypothetical gene, AF0830, of the A. fulgidus genomic sequence. The A. fulgidus ferric reductase shares amino acid sequence similarity with a family of NAD(P)H:FMN oxidoreductases but not with any ferric reductases suggesting that the A. fulgidus ferric reductase is a novel enzyme.

* This work was supported by National Institutes of Health Grant HL-16251 and National Sciennce Foundation Grant MCB-9631006 (to I. S.) and a grant from the United States Department of Commerce/NIST Cooperative Research Agreement No. 70NANB7H0009 (to H. G. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Microbiology and Molecular Genetics, 1602 Molecular Sciences Bldg., UCLA, Los Angeles, CA 90095. Tel.: 310-825-8085; Fax: 310-206-5231; E-mail: imkes@microbio.ucla.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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