The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 1.16.3.2     
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
References:
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 1.16.3.2 created 2014]
 
 


Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald