ExplorEnz: EC 7.2.1.3

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7.2.1.3

Accepted name:

ascorbate ferrireductase (transmembrane)

Reaction:

ascorbate_{[side 1]} + Fe(III)_{[side 2]} = monodehydroascorbate_{[side 1]} + Fe(II)_{[side 2]}

Other name(s):

cytochrome b₅₆₁ (ambiguous)

Systematic name:

Fe(III):ascorbate oxidorectuctase (electron-translocating)

Comments:

A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Flatmark, T. and Terland, O. Cytochrome b₅₆₁ of the bovine adrenal chromaffin granules. A high potential b-type cytochrome. Biochim. Biophys. Acta 253 (1971) 487–491. [DOI] [PMID: 4332308]
2.	McKie, A.T., Barrow, D., Latunde-Dada, G.O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T.J., Raja, K.B., Shirali, S., Hediger, M.A., Farzaneh, F. and Simpson, R.J. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 291 (2001) 1755–1759. [DOI] [PMID: 11230685]
3.	Su, D. and Asard, H. Three mammalian cytochromes b₅₆₁ are ascorbate-dependent ferrireductases. FEBS J. 273 (2006) 3722–3734. [DOI] [PMID: 16911521]
4.	Berczi, A., Su, D. and Asard, H. An Arabidopsis cytochrome b₅₆₁ with trans-membrane ferrireductase capability. FEBS Lett. 581 (2007) 1505–1508. [DOI] [PMID: 17376442]
5.	Wyman, S., Simpson, R.J., McKie, A.T. and Sharp, P.A. Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro. FEBS Lett. 582 (2008) 1901–1906. [DOI] [PMID: 18498772]
6.	Glanfield, A., McManus, D.P., Smyth, D.J., Lovas, E.M., Loukas, A., Gobert, G.N. and Jones, M.K. A cytochrome b₅₆₁ with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum. PLoS Negl. Trop. Dis. 4:e884 (2010). [DOI] [PMID: 21103361]

[EC 7.2.1.3 created 2011 as EC 1.16.5.1, transferred 2018 to EC 7.2.1.3]