Ascorbate ferrireductase (transmembrane)

Ascorbate ferrireductase (transmembrane) (EC 1.16.5.1, cytochrome b561) is an enzyme with systematic name Fe(III):ascorbate oxidorectuctase (electron-translocating).^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

ascorbate_[in] + Fe(III)_[out]

\rightleftharpoons

monodehydroascorbate radical_[in] + Fe(II)_[out] + H⁺_[in]

Ascorbate ferrireductase is a diheme cytochrome that acts on hexacyanoferrate(III) and other ferric chelates.

References

↑ Flatmark, T.; Terland, O. (1971). "Cytochrome b₅₆₁ of the bovine adrenal chromaffin granules. A high potential b-type cytochrome". Biochim. Biophys. Acta. 253 (2): 487–491. doi:10.1016/0005-2728(71)90052-1. PMID 4332308.
↑ 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.; Simpson, R.J. (2001). "An iron-regulated ferric reductase associated with the absorption of dietary iron". Science. 291 (5509): 1755–1759. doi:10.1126/science.1057206. PMID 11230685.
↑ Su, D.; Asard, H. (2006). "Three mammalian cytochromes b₅₆₁ are ascorbate-dependent ferrireductases". FEBS J. 273 (16): 3722–3734. doi:10.1111/j.1742-4658.2006.05381.x. PMID 16911521.
↑ Berczi, A.; Su, D.; Asard, H. (2007). "An Arabidopsis cytochrome b₅₆₁ with trans-membrane ferrireductase capability". FEBS Lett. 581 (7): 1505–1508. doi:10.1016/j.febslet.2007.03.006. PMID 17376442.
↑ Wyman, S.; Simpson, R.J.; McKie, A.T.; Sharp, P.A. (2008). "Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro". FEBS Lett. 582 (13): 1901–1906. doi:10.1016/j.febslet.2008.05.010. PMID 18498772.
↑ Glanfield, A.; McManus, D.P.; Smyth, D.J.; Lovas, E.M.; Loukas, A.; Gobert, G.N.; Jones, M.K. (2010). "A cytochrome b₅₆₁ with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum". PLOS Neglected Tropical Diseases. 4 (11): #e884–e884. doi:10.1371/journal.pntd.0000884. PMC 2982821. PMID 21103361.

External links

Ascorbate ferrireductase (transmembrane) at the US National Library of Medicine Medical Subject Headings (MeSH)

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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