Identification and characterization of a novel ferric reductase from the hyperthermophilic Archaeon Archaeoglobus fulgidus

Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing Archaeon, contains high Fe(3+)-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 e...

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Bibliographic Details

Published in:	The Journal of biological chemistry Vol. 274; no. 51; p. 36715
Main Authors:	Vadas, A, Monbouquette, H G, Johnson, E, Schröder, I
Format:	Journal Article
Language:	English
Published:	United States 17.12.1999
Subjects:	Archaeal Proteins - analysis Archaeal Proteins - genetics Archaeal Proteins - isolation & purification Archaeal Proteins - metabolism Archaeoglobus fulgidus - enzymology Electron Transport FMN Reductase Molecular Sequence Data NADH, NADPH Oxidoreductases - analysis NADH, NADPH Oxidoreductases - genetics NADH, NADPH Oxidoreductases - isolation & purification NADH, NADPH Oxidoreductases - metabolism Sequence Alignment Sequence Analysis
ISSN:	0021-9258
Online Access:	Get more information
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