EC 1.16.1.7 - Ferric-chelate reductase (NADH)
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ENZYME view
IntEnz Enzyme Nomenclature
EC 1.16.1.7
Names
Accepted name:
ferric-chelate reductase (NADH)
Other
names:
NADH:Fe3+-EDTA reductase
NADH2:Fe3+ oxidoreductase
ferric chelate reductase [ambiguous]
iron chelate reductase [ambiguous]
NADH:Fe3+ oxidoreductase
ferB (gene name)
Fe(II):NAD+ oxidoreductase
NADH2:Fe3+ oxidoreductase
ferric chelate reductase [ambiguous]
iron chelate reductase [ambiguous]
NADH:Fe3+ oxidoreductase
ferB (gene name)
Fe(II):NAD+ oxidoreductase
Systematic name:
Fe(II)-siderophore:NAD+ oxidoreductase
Reaction
- 2 Fe(II)-siderophore + NAD+ + H+ = 2 Fe(III)-siderophore + NADH
Cofactor
Comments:
Contains FAD. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The plant enzyme is involved in the transport of iron across plant plasma membranes. The enzyme from the bacterium Paracoccus denitrificans can also reduce chromate. cf. EC 1.16.1.9, ferric-chelate reductase (NADPH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
Links to other databases
Gene Ontology:
GO:0140618
CAS Registry Number:
122097-10-3
References
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Localization of donor and acceptor sites of NADH dehydrogenase activities using inside-out and right-side-out plasma membrane vesicles from plants.FEBS Lett. 239 : 23-28 (1988).
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NADH-dependent Fe3+ EDTA and oxygen reduction by plasma membrane vesicles from barley roots.Physiol. Plant. 75 : 245-254 (1989).
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Plasma membrane-bound NADH:Fe3+-EDTA reductase and iron deficiency in tomato (Lycopersicon esculentum). Is there a Turbo reductase?Physiol. Plant. 79 : 339-346 (1990).
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Pyridine nucleotide-dependent ferricyanide reduction associated with isolated plasma membranes of maize (Zea mays L.) roots.Protoplasma 135 : 144-154 (1986).
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Redox reactions of plasma membranes isolated from soybean hypocotyls by phase partition.Plant Sci. 48 : 1-10 (1986).
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Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans.Eur. J. Biochem. 271 : 553-562 (2004). [PMID: 14728682]
[EC 1.16.1.7 created 1992 as EC 1.6.99.13, transferred 2002 to EC 1.16.1.7, modified 2011, modified 2014]