IntEnz

EC 1.16.1.7 - Ferric-chelate reductase (NADH)

IntEnz Enzyme Nomenclature
EC 1.16.1.7

Names

Reaction

• 15061 [IUBMB]
  2

  a Fe(II)-siderophore

  a Fe(II)-siderophore

  GENERIC:11344

  Is ROOT: no
  ROOT compound: GENERIC:11341

  Number of residues: 1

  Fe2+ Fe(2+) Name origin: UniProt - CHECKED (C) CHEBI:29033 Formula: Fe Charge: 2 Position: undefined ChEBI compound status: CHECKED (C)

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  NAD⁺

  NAD(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:57540

  Formula: C21H26N7O14P2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  2

  a Fe(III)-siderophore

  a Fe(III)-siderophore

  GENERIC:11342

  Is ROOT: no
  ROOT compound: GENERIC:11341

  Number of residues: 1

  Fe3+ Fe(3+) Name origin: UniProt - CHECKED (C) CHEBI:29034 Formula: Fe Charge: 3 Position: undefined ChEBI compound status: CHECKED (C)

  +

  NADH

  NADH

  Name origin: UniProt - CHECKED (C)

  CHEBI:57945

  Formula: C21H27N7O14P2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Cofactor

• FAD

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

References

1. Askerlund, P., Larrson, C. and Widell, S.
   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).
2. Brüggemann, W. and Moog, P.R.
   NADH-dependent Fe³⁺ EDTA and oxygen reduction by plasma membrane vesicles from barley roots.
   Physiol. Plant. 75 : 245-254 (1989).
3. Brüggemann, W., Moog, P.R., Nakagawa, H., Janiesch, P. and Kuiper, P.J.C.
   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).
4. Buckhout, T.J. and Hrubec, T.C.
   Pyridine nucleotide-dependent ferricyanide reduction associated with isolated plasma membranes of maize (Zea mays L.) roots.
   Protoplasma 135 : 144-154 (1986).
5. Sandelius, A.S., Barr, R., Crane, F.L. and Morré, D.J.
   Redox reactions of plasma membranes isolated from soybean hypocotyls by phase partition.
   Plant Sci. 48 : 1-10 (1986).
6. Mazoch, J., Tesarik, R., Sedlacek, V., Kucera, I., Turanek, J.
   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]