@article {613,
	title = {Characterization of a membrane-bound NADH-dependent Fe(3+) reductase from the dissimilatory Fe(3+)-reducing bacterium Geobacter sulfurreducens.},
	journal = {FEMS Microbiol Lett},
	volume = {185},
	year = {2000},
	month = {2000 Apr 15},
	pages = {205-11},
	abstract = {Geobacter sulfurreducens produces a single, membrane-associated Fe(3+) reductase activity when grown on fumarate or Fe(3+). The activity was initially isolated by solubilization of membranes with the non-ionic detergent dodecyl-beta-D-maltoside, and partially purified by a combination of ion exchange chromatography and preparative non-denaturing gel electrophoresis. Molecular mass of the reductase, as determined by gel filtration chromatography, was approximately 300 kDa. Cofactor analysis of the purified reductase demonstrates that it contains a hemoprotein and flavin adenine dinucleotide. Kinetic and inhibitor studies show that the reductase is specific for NADH as electron donor, and confirm that the reductase enzymatically reduces Fe(3+). The cytochrome associated with the complex undergoes a reoxidation upon addition of Fe(3+) compounds, indicating an ability to pass reducing equivalents to Fe(3+). This is the first description of a purified NADH-dependent Fe(3+) reductase from a microorganism capable of coupling Fe(3+) reduction to growth.},
	keywords = {Cell Membrane, Deltaproteobacteria, Ferric Compounds, FMN Reductase, NADH, NADPH Oxidoreductases, Oxidation-Reduction},
	issn = {0378-1097},
	author = {Magnuson, T S and Hodges-Myerson, A L and Lovley, D R}
}
