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Information on EC 1.6.2.2 - cytochrome-b5 reductase
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1.6.2.2 cytochrome-b5 reductaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.6.2.2
- erythrocyte
- methemoglobinemia
-
nadph-cytochrome
- hereditary
- reductases
-
cyanosis
- fad
- ferricyanide
- flavoproteins
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desaturation
- dt-diaphorase
- aniline
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amidoxime
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methb
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hemolysate
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bioreductive
- n-demethylase
- aminopyrine
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marc
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n-hydroxylated
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mixed-function
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nadh-binding
- methaemoglobin
- medicine
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oxyhemoglobin
- diagnostics
- analysis
- industry
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadh-cytochrome b5 reductase, cytochrome b5 reductase, methemoglobin reductase, cyb5r3, ncb5or, nadh cytochrome b5 reductase, nadh:cytochrome b5 reductase, cyb5r2, cytochrome-b5 reductase, cyb5r, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
B5R
cb5r
CBR
CBR1
CyB5R
CYB5R3
cytochrome b5 reductase
cytochrome b5 reductase 3
dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase
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NADH cytochrome B5 reductase
NADH-cytochrome b5 reductase
NADH-cytochrome-b5 reductase
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NADH-dependent cytochrome b5 reductase
NADH-ferricyanide reductase
NADH-ferricytochrome b5 oxidoreductase
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NADH:cytochrome b5 reductase
NADH:ferricytochrome b5 oxidoreductase
P34/P32
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P35
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reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase
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reductase, cytochrome b5
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B5R
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cytochrome b5 reductase
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NADH-cytochrome b5 reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
ordered bi bi mechanism
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
electron-transport chain from NADH to a terminal oxidase desaturase, proposed electron transfer mechanism
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
reaction mechanism, overview
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NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
Y93 forms contact with the FAD, but neither P92 nor Y93 preceeding the conserved motif RxYTSxxSN coordinating flavin binding are critical for flavin incorporation
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
NADH:ferricytochrome-b5 oxidoreductase
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9032-25-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dihydro-8-(4-methylpiperazin-1-yl)-4-phenylimidazol[3,2-e]pyrazine 5-oxide + NADH
1,2-dihydro-8-(4-methylpiperazin-1-yl)-4-phenylimidazol[3,2-e]pyrazine + NAD+
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potential bioreductive drug, trivial name RB90740
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?
2 ferricytochrome b5 + NADPH
2 ferrocytochrome b5 + NADP+ + H+
with NADPH the enzyme shows about 20% of the activity with NADH
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-
?
2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt + NADH
?
-
-
-
?
aquacobalamin + NADH
reduced aquacobalamin + NAD+
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in the presence of outer membrane cytochrome b, no activity with cyanocobalamin
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?
Fe3+-ammonium sulfate + NADH
Fe2+-ammonium sulfate + NAD+
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strongly elevated by the addition of cytochrome b5
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?
Fe3+-histidine + NADH
Fe2+-histidine + NAD+
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strongly elevated by the addition of cytochrome b5
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?
Fe3+-nitrilotriacetate + NADH
Fe2+-nitrilotriacetate + NAD+
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in the presence of cytochrome b5, iron chelate reduction in descending order: Fe3+-nitrolotriacetate, Fe3+-ADP, Fe3+-diphosphate, Fe3+-citrate
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?
ferricytochrome b5 + 4-(5-(4-[amino(hydroxyamino)methyl]phenyl)-2-furyl)-N'-hydroxybenzenecarboximidamide
ferrocytochrome b5 + ?
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metabolite of DB289, an antimicrobial prodrug of furamidine
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?
ferricytochrome b5 + 4-(5-(4-[amino(hydroxyamino)methyl]phenyl)-2-furyl)-N'-methoxybenzenecarboximidamide
ferrocytochrome b5 + ?
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metabolite of DB289, an antimicrobial prodrug of furamidine
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?
ferricytochrome b5 + N-hydroxy-2-amino-1-methyl-6-phenylimidazol[4,5-b]pyridine
ferrocytochrome b5 + ?
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arylhydroxylamine carcinogen found in grilled meat
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?
ferricytochrome b5 + N-hydroxy-4-aminobiphenyl
ferrocytochrome b5 + ?
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arylhydroxylamine carcinogen found in cigarette smoke
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?
methemoglobin-ferrocyanide complex + NADH
reduced methemoglobin-ferrocyanide complex + NAD+
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?
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
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?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
NADH + oxidized nitroblue tetrazolium
NAD+ + H+ + reduced nitroblue tetrazolium
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?
sulfamethoxazole hydroxylamine + NADH
?
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in the presence of cytochrome b5
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?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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no acceptors: ubiquinone-30, menadione, dihydrofolate, lipoamide
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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poor donor: NADPH
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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artificial acceptor: ferricyanide, high reactivity with NADPH as electron donor
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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poor electron acceptors: methylene blue, ferricytochrome c, O2, oxidized glutathione, methemoglobin
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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artificial electron acceptor in the presence of menadione: cytochrome c
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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additional electron donors: deamino-NADH, 3-acetylpyridine-NADH
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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artificial acceptors: p-benzoquinone, 5-hydroxy-1,4-naphthoquinone, nitroblue-tetrazolium
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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additional acceptor: methemoglobin-ferrocyanide complex
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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involved in metabolism of endogenous compounds such as steroids, drugs, carcinogens, environmental pollutants
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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enzyme participates in methemoglobin reduction in erythrocytes, in other tissues it plays a role in elongation and desaturation of fatty acids, P-450 mediated drug metabolism and cholesterol biosynthesis as part of the microsomal electron transfer system
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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soluble form of erythrocytes: reduction of methemoglobin
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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soluble form of erythrocytes: reduction of methemoglobin
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, enzyme in presence of cytochrome b5 supports activity of CYP2E1
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, participates in the regeneration of vitamin E and of ascorbate, maintains antioxidant levels and is therefore involved in the protection of membrane lipids from peroxidation, considered as a constitutive housekeeping enzyme
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
recessive congenital methaemoglobinaemia, is caused by NADH-cytochrome b5 reductase deficiency. Two distinct clinical forms, types I and II, are recognized, both characterized by cyanosis from birth. In type II, the cyanosis is accompanied by neurological impairment and reduced life expectancy
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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the electrostatic interactions between the lysyl residues (K42, K126, K163, and K164) in the enzyme and the carboxyl groups (E47, E48, E52, E60, and D64) of cytochrome b5 keep the proteins tightly complexed and are suitable for electron transfer, reaction mechanism, overview
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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potassium ferricyanide, cytochrome b5, or NADH-2,6-dichlorophenol-indophenol can act as electron acceptors
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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uses both NADH and NADPH as electron donors, artificial acceptors: ferricyanide, 2,6-dichlophenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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-
-
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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low activity with trypsin-solubilized cytochrome b5
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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additional acceptor: hemin
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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poor donor: NADPH
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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additional acceptor: methemoglobin-ferrocyanide complex
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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artificial acceptor: ferricyanide
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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additional acceptor: methemerythrin
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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recombinant enzyme, very low activity with NADPH
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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involved in desaturation of fatty acids
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, enzyme defects causes methemoglobinemia type I or type II
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-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II
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-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
enzyme complex drives the entire sterol 14-demethylation reaction
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
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involved in desaturation of fatty acids
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?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
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?