CYB5Rs reduce MetHb to HbA

Stable Identifier
Reaction [transition]
Homo sapiens
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NADH-Cytochrome b5 reductases (CYB5Rs), flavoproteins consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyse electron transfer from the two-electron carrier NADH to the one-electron carrier ferricytochrome b5 ((Fe(3+)Cb5), forming ferrocytochrome b5 ((Fe(2+)Cb5) (Zhu et al. 1999, Baker et al. 2005, Zhu et al. 2004). CYB5Rs participate in fatty acid synthesis, cholesterol synthesis and xenobiotic oxidation as members of the electron transport chain on the endoplasmic reticulum membrane. In erythrocytes, CYB5Rs participate in the reduction of methemoglobin (MetHb) to hemoglobin A (HbA).
Literature References
PubMed ID Title Journal Year
10611283 Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells

Bunn, HF, Huang, S, Yoon, HW, Zhu, H, Qiu, H

Proc. Natl. Acad. Sci. U.S.A. 1999
15131110 NCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic reticulum

Berchner-Pfannschmidt, U, Ladoux, A, Jackson, TA, Acker, H, Cross, AR, Larade, K, Xie, J, Rodgers, KR, Fandrey, J, Zhu, H, Bunn, HF, Lukat-Rodgers, GS

J. Biol. Chem. 2004
15858218 Identification of cytochrome-b5 reductase as the enzyme responsible for NADH-dependent lucigenin chemiluminescence in human spermatozoa

Curry, BJ, Hetherington, L, Krutskikh, A, Aitken, RJ, Baker, MA

Biol. Reprod. 2005
Catalyst Activity

cytochrome-b5 reductase activity, acting on NAD(P)H of CYB5Rs [endoplasmic reticulum membrane]

Orthologous Events
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