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Information on EC 1.6.2.2 - cytochrome-b5 reductase and Organism(s) Rattus norvegicus and UniProt Accession Q68EJ0

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EC Tree
     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.2 With a heme protein as acceptor
                1.6.2.2 cytochrome-b5 reductase
IUBMB Comments
A flavoprotein (FAD).
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: Q68EJ0
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYB5R3
cytochrome b5 reductase
cytochrome b5 reductase 3
-
-
dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase
-
-
-
-
NADH cytochrome B5 reductase
-
NADH-cytochrome b5 reductase
NADH-cytochrome-b5 reductase
-
-
-
-
NADH-ferricytochrome b5 oxidoreductase
-
-
-
-
NADH:cytochrome b5 reductase
-
-
P34/P32
-
-
-
-
P35
-
-
-
-
reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase
-
-
-
-
reductase, cytochrome b5
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
NADH:ferricytochrome-b5 oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9032-25-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
show the reaction diagram
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
show the reaction diagram
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
2 ferricytochrome c + NADH + H+
2 ferrocytochrome c + NAD+
show the reaction diagram
-
-
-
-
?
5alpha-dihydrotestosterone + acceptor
?
show the reaction diagram
-
-
-
-
r
aquacobalamin + NADH
reduced aquacobalamin + NAD+
show the reaction diagram
-
in the presence of outer membrane cytochrome b, no activity with cyanocobalamin
-
?
Fe3+-ammonium sulfate + NADH
Fe2+-ammonium sulfate + NAD+
show the reaction diagram
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
show the reaction diagram
Fe3+-histidine + NADH
Fe2+-histidine + NAD+
show the reaction diagram
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-nitrilotriacetate + NADH
Fe2+-nitrilotriacetate + NAD+
show the reaction diagram
-
in the presence of cytochrome b5, iron chelate reduction in descending order: Fe3+-nitrolotriacetate, Fe3+-ADP, Fe3+-diphosphate, Fe3+-citrate
-
?
NADH + ferricytochrome b5
NAD+ + H+ + 2 ferrocytochrome b5
show the reaction diagram
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
show the reaction diagram
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
show the reaction diagram
-
-
-
-
?
NADH + ferricytochrome c
NAD+ + H+ + ferrocytochrome c
show the reaction diagram
NADH + H+ + 2 O2
?
show the reaction diagram
-
-
-
-
?
NADH + methemoglobin
NAD+ + hemoglobin
show the reaction diagram
-
-
-
-
?
NADH + testosterone
?
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
show the reaction diagram
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
show the reaction diagram
5alpha-dihydrotestosterone + acceptor
?
show the reaction diagram
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
show the reaction diagram
-
-
-
-
?
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
show the reaction diagram
-
-
-
-
?
NADH + methemoglobin
NAD+ + hemoglobin
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-(p-fluorosulfonylbenzoyl)-adenosine
-
-
6-Propyl-2-thiouracil
-
about 20% residual activity at 0.009 mM
dicoumarol
-
-
ebselen
-
almost complete inhibition at 0.02 mM
Mepacrin
-
-
Mersalyl
-
complete inhibition at 1.0 mM
NAD+
competitive, stronger inhibition of mutant enzymes compared to wild type enzyme
p-chloromercuribenzoate
-
complete inhibition at 0.4 mM
Pentachlorophenol
-
-
quercetin
-
about 20% residual activity at 0.02 mM
Thenoyltrifluoroacetone
-
-
ZINC39395747
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0419
aquacobalamin
-
-
0.003 - 0.012
cytochrome b5
-
0.005 - 0.76
ferricyanide
0.01 - 0.013
ferricytochome b5
-
0.01 - 0.015
ferricytochrome b5
0.007
ferricytochrome c
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.001 - 0.107
ferrocytochrome b5
0.003 - 1.077
NADH
0.001 - 2.317
NADPH
0.025 - 0.089
testosterone
-
depending on phosphate concentration
additional information
additional information
-
detailed analysis of biphasic rate of reduction of cytochrome b5 in membranes. The initial rapid phase is completed within 10 msec and over 90% of cytochrome b5 are reduced in 40 msec. Evaluation of data in terms of two-dimensional random walk model
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12 - 880
ferricyanide
33 - 417
ferricytochome b5
-
1 - 400
ferricytochrome b5
10 - 400
ferrocytochrome b5
250 - 800
NADH
5.2 - 550
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.109
-
reduction of aquacobalamin
1400
-
recombinant enzyme
1470
-
enzyme from liver plasma membrane
2480
-
reduction of ferricyanide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytochrome b5/cytochrome b5 reductase fusion protein, exists also as a variant where the whole exon 12 is deleted
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
transcripts of L, X and Y mRNAs are detected
Manually annotated by BRENDA team
-
transcripts of L, X and Y mRNAs are detected
Manually annotated by BRENDA team
-
neuronal synaptic plasma membrane vesicles
Manually annotated by BRENDA team
-
transcripts of L, X, R and Y mRNAs are detected
Manually annotated by BRENDA team
additional information
exon 12 deletion variant is not found in kidney, lung, liver, and heart
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
2 forms in erythrocytes: a soluble and a membrane-bound enzyme which represents the majority
Manually annotated by BRENDA team
-
neuronal synaptic plasma membrane vesicles
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the NADH/cytochrome b5/enzyme system can act as the sole electron donor both for the first and second reduction of cytochrome P450 1A1 during the oxidation of benzo[a]pyrene in vitro
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NB5R4_RAT
520
0
58835
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
sedimentation equilibrium
28000
-
gel filtration
30000
30588
-
1 * 30588, recombinant enzyme, MALDI-TOF mass spectrometry
32000
-
1 * 32000, SDS-PAGE
33100
-
1 * 33100, SDS-PAGE
34000
x * 34000, Western blot analysis
42800
-
x * 42800, chimeric protein NADH-cytochrome b5 reductase-cytochrome b5, confirmed by SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop method
-
sitting drop method, complete data set collected for the D239T mutant enzyme
sitting drop method, reservoir: 8% poly ethylene glycol 6000, 5% 2-methyl-2,4-pentanediol in 100 mM 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid, pH 7.5, X-ray structure, resolution: enzyme 2.0 A, enzyme-NAD+ complex, 2.3 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D239E
decreased activity with NADH and NADPH
D239S
significantly increased activity with NADPH
D239S/F251R
specific for NADPH
D239S/F251Y
bispecific for NADH and NADPH
D239T
specific for NADPH, 11fold preference for NADPH over NADH
D239T/F251R
specific for NADPH
F251R
minor effects on activity
F251Y
minor effects on activity
G179A
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
G179P
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
G179T
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
G179V
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
K110A
strongly reduced kcat for ferricyanide and cytochrome b5
K110E
strongly reduced kcat for ferricyanide and cytochrome b5
K110H
strongly reduced kcat for ferricyanide and cytochrome b5
K110Q
very low kcat for ferricyanide and cytochrome b5
K110R
reduced kcat for ferricyanid and cytochrome b5
L148P
31% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+
P144L
28% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+
P144L/L148P
8% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+
P92A
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
P92G
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
P92S
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
R159
deletion mutant, could not be successfully expressed
S127P
-
caused methemoglobinemia type II, FAD is displaced from its binding site by NADH, Km for NADH is strongly increased
Y93A
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93D
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93F
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93H
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93S
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93W
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
additional information
-
a chimeric protein NADH-cytochrome b5 reductase-cytochrome b5 is constructed
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation caused by solubilization with detergents, activity restored by phosphatidylcholine
-
phosphate stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen, 50 mM potassium phosphate buffer, pH 7.5, 1 mM EDTA, several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric protein NADH-cytochrome b5 reductase-cytochrome b5
-
lysosome-solubilization
-
polyethylene glycol precipitation, DEAE-cellulose, hydroxylapatite, ADP-agarose
-
recombinant enzyme
recombinant enzyme, affinity chromatography on 5'-ADP-agarose
-
recombinant enzymes
recombinant enzymes purified from Escherichia coli
-
Triton X-100, anion exchange chromatography, gel filtration
-
wild-type, K110R, K110H, K110A, K110E and K110Q mutant enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)-RIL
expression in Escherichia coli
expression of a soluble fusion protein comprising a b-type cytochrome containing domain and a FAD-containing domain
-
expression of wild-type, K110R, K110H, K110A, K110E and K110Q mutant enzymes in Escherichia coli
mutant enzymes expressed in Escherichia coli BL21(DE3)-RIL as His-tag fusion proteins
wild type and mutant enzyme expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significant increase in the activity of cytochrome b5 reductase is observed after trichloroaceticacid treatment at 0.2% (w/v) (about 12 mM) concentration in drinking water ad libitum for 60 days as compared to control groups
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
detailed analysis of biphasic rate of reduction of cytochrome b5 in membranes with evaluation of data in terms of two-dimensional random walk model. The initial rapid phase is completed within 10 msec and over 90% of cytochrome b5 are reduced in 40 msec
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borgese, N.; Longhi, R.
Both the outer mitochondrial membrane and the microsomal forms of cytochrome b5 reductase contain covalently bound myristic acid. Quantitative analysis on the polyvinylidene difluoride-immobilized proteins
Biochem. J.
266
341-347
1990
Rattus norvegicus
Manually annotated by BRENDA team
Borgese, N.; Pietrini, G.
Distribution of the integral membrane protein NADH-cytochrome b5 reductase in rat liver cells, studied with a quantitative radioimmunoblotting assay
Biochem. J.
239
393-403
1986
Rattus norvegicus
Manually annotated by BRENDA team
Golf, S.W.; Graf, V.; Rempeters, G.; Mersdorf, S.
Properties and biochemical characterization of NADH 5alpha-reductase from rat liver microsomes
Biol. Chem. Hoppe-Seyler
366
647-653
1985
Rattus norvegicus
Manually annotated by BRENDA team
Borgese, N.; Macconi, D.; Parola, L.; Pietrini, G.
Rat erythrocyte NADH-cytochrome b5 reductase. Quantitation and comparison between the membrane-bound and soluble forms using an antibody against the rat liver enzyme
J. Biol. Chem.
257
13854-13861
1982
Rattus norvegicus
Manually annotated by BRENDA team
Takesue, S.; Omura, T.
Purification and properties of NADH-cytochrome b5 reductase solubilized by lysosomes from rat liver microsomes
J. Biochem.
67
267-276
1970
Rattus norvegicus
Manually annotated by BRENDA team
Strittmatter, P.
Microsomal cytochrome b5 and cytochrome b5 reductase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
8
113-145
1963
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Oshino, N.; Sato, R.
Stimulation by phenols of the reoxidation microsomal bound cytochrome b5 and its implication to fatty acid desaturation
J. Biochem.
69
169-180
1971
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Mota Vieira, L.; Kaplan, J.C.; Kahn, A.; Leroux, A.
Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts resulting from multiple alternative first exons
Eur. J. Biochem.
220
729-737
1994
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Yang, M.X.; Cederbaum, A.I.
Fractionation of liver microsomes with polyethylene glycol and purification of NADH-cytochrome b5 oxidoreductase and cytochrome b5
Arch. Biochem. Biophys.
315
438-444
1994
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Saido, H.; Watanabe, F.; Tamura, Y.; Miyatake, K.; Ito, A.; Yubisui, T.; Nakano, Y.
Cytochrome b5-like hemoprotein/cytochrome b5 reductase complex in rat liver mitochondria has NADH-linked aquacobalamin reductase activity
J. Nutr.
124
1037-1040
1994
Rattus norvegicus
Manually annotated by BRENDA team
Miura, A.; Tampo, Y.; Yonaha, M.
The reducing ability of iron chelates by NADH-cytochrome B5 reductase or cytochrome B5 responsible for NADH-supported lipid peroxidation
Biochem. Mol. Biol. Int.
37
141-150
1995
Rattus norvegicus
Manually annotated by BRENDA team
Kim, C.; Crane, F.L.; Becker, G.W.; Morre, D.J.
Purification of NADH-cytochrome b5 reductase from rat liver plasma membranes
Protoplasma
184
111-117
1995
Rattus norvegicus
-
Manually annotated by BRENDA team
Barber, M.J.; Quinn, G.B.
High-level expression in Escherichia coli of the soluble, catalytic domain of rat hepatic cytochrome b5 reductase
Protein Expr. Purif.
8
41-47
1996
Rattus norvegicus
Manually annotated by BRENDA team
Yang, M.X.; Cederbaum, A.I.
Interaction of ferric complexes with NADH-cytochrome b5 reductase and cytochrome b5: lipid peroxidation, H2O2 generation, and ferric reduction
Arch. Biochem. Biophys.
331
69-78
1996
Rattus norvegicus
Manually annotated by BRENDA team
Bewley, M.C.; Marohnic, C.C.; Barber, M.J.
The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent
Biochemistry
40
13574-13582
2001
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Davis, C.A.; Dhawan, I.K.; Johnson, M.K.; Barber, M.J.
Heterologous expression of an endogenous rat cytochrome b5/cytochrome b5 reductase fusion protein: Identification of histidines 62 and 85 as the heme axial ligands
Arch. Biochem. Biophys.
400
63-75
2002
Rattus norvegicus
Manually annotated by BRENDA team
Davis, C.A.; Crowley, L.J.; Barber, M.J.
Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*
Arch. Biochem. Biophys.
431
233-244
2004
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Marohnic, C.C.; Bewley, M.C.; Barber, M.J.
Engineering and characterization of a NADPH-utilizing cytochrome b5 reductase
Biochemistry
42
11170-11182
2003
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Bewley, M.C.; Davis, C.A.; Marohnic, C.C.; Taormina, D.; Barber, M.J.
The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site
Biochemistry
42
13145-13151
2003
Rattus norvegicus
Manually annotated by BRENDA team
Curry, B.J.; Roman, S.D.; Wallace, C.A.; Scott, R.; Miriami, E.; Aitken, R.J.
Identification and characterization of a novel splice variant of mouse and rat cytochrome b5/cytochrome b5 reductase
Genomics
83
425-438
2004
Mus musculus (Q3TDX8), Mus musculus, Rattus norvegicus (Q68EJ0)
Manually annotated by BRENDA team
Roma, G.W.; Crowley, L.J.; Davis, C.A.; Barber, M.J.
Mutagenesis of glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase
Biochemistry
44
13467-13476
2005
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Marohnic, C.C.; Crowley, L.J.; Davis, C.A.; Smith, E.T.; Barber, M.J.
Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis
Biochemistry
44
2449-2461
2005
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Tonegawa, Y.; Umeda, N.; Hayakawa, T.; Ishibashi, T.
Evaluation of data in terms of two-dimensional random walk model: interaction between NADH-cytochrome b5 reductase and cytochrome b5
Biomed. Res.
26
207-212
2005
Rattus norvegicus
Manually annotated by BRENDA team
Colombo, S.; Longhi, R.; Alcaro, S.; Ortuso, F.; Sprocati, T.; Flora, A.; Borgese, N.
N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning
J. Cell Biol.
168
735-745
2005
Rattus norvegicus
Manually annotated by BRENDA team
Percy, M.J.; Lappin, T.R.
Recessive congenital methaemoglobinaemia: cytochrome b(5) reductase deficiency
Br. J. Haematol.
141
298-308
2008
Homo sapiens (P00387), Homo sapiens, Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Asada, T.; Nagase, S.; Nishimoto, K.; Koseki, S.
Molecular dynamics simulation study on stabilities and reactivities of NADH cytochrome B5 reductase
J. Phys. Chem. B
112
5718-5727
2008
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Yantsevich, A.V.; Gilep, A.A.; Usanov, S.A.
Mechanism of electron transfer in fusion protein cytochrome b5-NADH-cytochrome b5 reductase
Biochemistry (Moscow)
73
1096-1107
2008
Rattus norvegicus
Manually annotated by BRENDA team
Samhan-Arias, A.K.; Garcia-Bereguiain, M.A.; Martin-Romero, F.J.; Gutierrez-Merino, C.
Clustering of plasma membrane-bound cytochrome b5 reductase within lipid raft microdomains of the neuronal plasma membrane
Mol. Cell. Neurosci.
40
14-26
2009
Rattus norvegicus (P20070)
Manually annotated by BRENDA team
Marques-da-Silva, D.; Samhan-Arias, A.K.; Tiago, T.; Gutierrez-Merino, C.
L-type calcium channels and cytochrome b5 reductase are components of protein complexes tightly associated with lipid rafts microdomains of the neuronal plasma membrane
J. Proteomics
73
1502-1510
2010
Rattus norvegicus
Manually annotated by BRENDA team
Siddique, Y.; Ara, G.; Gupta, J.; Beg, T.; Afzal, M.
Estimation of cytochrome b5 reductase activity in red blood cells of Rattus norvegicus after the treatment of trichloroacetic acid
Pharmacologyonline
3
986-990
2009
Rattus norvegicus
-
Manually annotated by BRENDA team
Stiborova, M.; Indra, R.; Moserova, M.; Frei, E.; Schmeiser, H.H.; Kopka, K.; Philips, D.H.; Arlt, V.M.
NADH cytochrome b5 reductase and cytochrome b5 can act as sole electron donors to human cytochrome P450 1A1-mediated oxidation and DNA adduct formation by benzo[a]pyrene
Chem. Res. Toxicol.
29
1325-1334
2016
Rattus norvegicus
Manually annotated by BRENDA team
Rahaman, M.M.; Nguyen, A.T.; Miller, M.P.; Hahn, S.A.; Sparacino-Watkins, C.; Jobbagy, S.; Carew, N.T.; Cantu-Medellin, N.; Wood, K.C.; Baty, C.J.; Schopfer, F.J.; Kelley, E.E.; Gladwin, M.T.; Martin, E.; Straub, A.C.
Cytochrome b5 reductase 3 modulates soluble guanylate cyclase redox state and cGMP signaling
Circ. Res.
121
137-148
2017
Rattus norvegicus
Manually annotated by BRENDA team
Nikiforova, A.B.; Saris, N.E.; Kruglov, A.G.
External mitochondrial NADH-dependent reductase of redox cyclers VDAC1 or Cyb5R3?
Free Radic. Biol. Med.
74
74-84
2014
Rattus norvegicus
Manually annotated by BRENDA team
Kollipara, S.; Tatireddy, S.; Pathirathne, T.; Rathnayake, L.K.; Northrup, S.H.
Contribution of electrostatics to the kinetics of electron transfer from NADH-cytochrome b5 reductase to Fe(III)-cytochrome b5
J. Phys. Chem. B
120
8193-8207
2016
Rattus norvegicus
Manually annotated by BRENDA team
Samhan-Arias, A.K.; Fortalezas, S.; Cordas, C.M.; Moura, I.; Moura, J.J.G.; Gutierrez-Merino, C.
Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c
Redox Biol.
15
109-114
2018
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team