The Enzyme Database

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Accepted name: bacterial non-heme ferritin
Reaction: 4 Fe(II) + O2 + 6 H2O = 4 [FeO(OH)] + 8 H+ (overall reaction)
(1a) 2 Fe(II) + O2 + 4 H2O = 2 [FeO(OH)] + 4 H+ + H2O2
(1b) 2 Fe(II) + H2O2 + 2 H2O = 2 [FeO(OH)] + 4 H+
Glossary: [FeO(OH)] = iron(III) oxide-hydroxide
Other name(s): FtnA; HuHF
Systematic name: Fe(II):oxygen oxidoreductase ([FeO(OH)]core-producing)
Comments: Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. Thousands of mineralized iron atoms are stored within the core of the structure. The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Hudson, A.J., Andrews, S.C., Hawkins, C., Williams, J.M., Izuhara, M., Meldrum, F.C., Mann, S., Harrison, P.M. and Guest, J.R. Overproduction, purification and characterization of the Escherichia coli ferritin. Eur. J. Biochem. 218 (1993) 985–995. [PMID: 8281950]
2.  Stillman, T.J., Hempstead, P.D., Artymiuk, P.J., Andrews, S.C., Hudson, A.J., Treffry, A., Guest, J.R. and Harrison, P.M. The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe3+ and Zn2+ derivatives. J. Mol. Biol. 307 (2001) 587–603. [PMID: 11254384]
3.  Bou-Abdallah, F., Yang, H., Awomolo, A., Cooper, B., Woodhall, M.R., Andrews, S.C. and Chasteen, N.D. Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA). Biochemistry 53 (2014) 483–495. [PMID: 24380371]
[EC created 2014]

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