Abstract
Microsomal NADH:Fe(III)-chelate reductase (NFR) of maize roots has been purified as a monomeric flavoprotein of 32 kDa with non-covalently bound FAD. In the presence of NADH, NFR efficiently reduced the physiological iron-chelate Fe(III)-citrate (K[cat]/K[m](Fe(III)-citrate) = 6.0 X 10[6] M[-1] S[-1]) with a sequential reaction mechanism. Purified NFR was totally inhibited by the sulfhydryl reagent PHMB at 10(-9) M, and it could use cyt b5 as alternative electron acceptor with a maximal reduction rate as high as with Fe(III)-citrate. We conclude that in maize roots the reduction of Fe(III)-citrate is chiefly performed by a cytochrome b5 reductase, mostly associated with intracellular membranes and in part with the plasma membrane.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Membrane / enzymology
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Cytochrome Reductases / metabolism*
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Cytochrome-B(5) Reductase
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Enzyme Inhibitors / pharmacology
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FMN Reductase*
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Ferric Compounds / metabolism
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Fluorometry
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Hydroxymercuribenzoates / pharmacology
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Kinetics
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Microsomes / chemistry
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Microsomes / enzymology
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NAD / metabolism
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NADH, NADPH Oxidoreductases / chemistry
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NADH, NADPH Oxidoreductases / drug effects
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NADH, NADPH Oxidoreductases / metabolism*
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Organomercury Compounds / pharmacology
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Plant Roots / enzymology*
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Zea mays / enzymology*
Substances
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Enzyme Inhibitors
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Ferric Compounds
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Hydroxymercuribenzoates
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Organomercury Compounds
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NAD
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4-hydroxymercuribenzoate
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ferric citrate
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FMN Reductase
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NADH, NADPH Oxidoreductases
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Cytochrome Reductases
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Cytochrome-B(5) Reductase
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ferric citrate iron reductase