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2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
2 ferricytochrome c + NADH + H+
2 ferrocytochrome c + NAD+
-
-
-
-
?
5alpha-dihydrotestosterone + acceptor
?
-
-
-
-
r
aquacobalamin + NADH
reduced aquacobalamin + NAD+
-
in the presence of outer membrane cytochrome b, no activity with cyanocobalamin
-
?
Fe3+-ammonium sulfate + NADH
Fe2+-ammonium sulfate + NAD+
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
Fe3+-histidine + NADH
Fe2+-histidine + NAD+
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-nitrilotriacetate + NADH
Fe2+-nitrilotriacetate + NAD+
-
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
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
-
-
-
-
?
NADH + ferricytochrome c
NAD+ + H+ + ferrocytochrome c
NADH + H+ + 2 O2
?
-
-
-
-
?
NADH + methemoglobin
NAD+ + hemoglobin
-
-
-
-
?
NADH + testosterone
?
-
-
-
-
r
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
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
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
?
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+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
recombinant enzyme, very low activity with NADPH
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in desaturation of fatty acids
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
-
-
?
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
-
-
?
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
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
in the presence of outer membrane cytochrome b
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
cytochrome b5/cytochrome b5 reductase FAD-domain-fusion protein, NADPH is preferred
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
-
reconstituted system containing NADH, cytochrome b5 reductase, cytochrome b5 and microsomal lipids catalyzes lipid peroxidation in the presence of ferric-ATP, ferric-histidine and ferric-ammonium sulfate
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
-
ferric-EDTA is not reduced
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
r
NADH + ferricytochrome c
NAD+ + H+ + ferrocytochrome c
-
-
-
-
?
NADH + ferricytochrome c
NAD+ + H+ + ferrocytochrome c
-
-
-
-
r
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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
0.025 - 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
-
0.003
cytochrome b5
K110Q mutant enzyme
-
0.004
cytochrome b5
K110E mutant enzyme
-
0.009
cytochrome b5
K110R mutant enzyme
-
0.009
cytochrome b5
K110A mutant enzyme
-
0.01
cytochrome b5
recombinant wild-type enzyme
-
0.012
cytochrome b5
K110H mutant enzyme
-
0.005
ferricyanide
K110R mutant enzyme
0.0058
ferricyanide
mutant Y93S, pH 7.0, 25°C
0.006
ferricyanide
recombinant wild-type enzyme
0.0066
ferricyanide
mutant Y93F, pH 7.0, 25°C
0.0068
ferricyanide
mutant Y93W, pH 7.0, 25°C
0.007
ferricyanide
-
recombinant enzyme
0.007
ferricyanide
-
pH 7.0, wild type enzyme
0.007
ferricyanide
mutant G179P, pH 7.0
0.007
ferricyanide
mutant G179V, pH 7.0
0.0071
ferricyanide
wild-type, pH 7.0, 25°C
0.0074
ferricyanide
mutant P92A, pH 7.0, 25°C
0.0078
ferricyanide
mutant P92S, pH 7.0, 25°C
0.008
ferricyanide
wild-type, pH 7.0
0.008
ferricyanide
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.008
ferricyanide
L148P mutant enzyme, pH 7.0, 25°C
0.008
ferricyanide
P144L mutant enzyme, pH 7.0, 25°C
0.008
ferricyanide
P144L/L148P mutant enzyme, pH 7.0, 25°C
0.008
ferricyanide
-
pH 7.0, S127P mutant enzyme
0.008
ferricyanide
wild type enzyme, pH 7.0, 25°C
0.008
ferricyanide
mutant G179A, pH 7.0
0.008
ferricyanide
mutant G179T, pH 7.0
0.008
ferricyanide
mutant P92G, pH 7.0, 25°C
0.0083
ferricyanide
mutant Y93D, pH 7.0, 25°C
0.0083
ferricyanide
mutant Y93H, pH 7.0, 25°C
0.0086
ferricyanide
mutant Y93A, pH 7.0, 25°C
0.05
ferricyanide
K110H mutant enzyme
0.37
ferricyanide
K110E mutant enzyme
0.38
ferricyanide
K110A mutant enzyme
0.76
ferricyanide
K110Q mutant enzyme
0.01
ferricytochome b5
L148P mutant enzyme, pH 7.0, 25°C
-
0.012
ferricytochome b5
P144L mutant enzyme, pH 7.0, 25°C
-
0.013
ferricytochome b5
P144L/L148P mutant enzyme, pH 7.0, 25°C
-
0.013
ferricytochome b5
wild type enzyme, pH 7.0, 25°C
-
0.01
ferricytochrome b5
mutant Y93D, pH 7.0, 25°C
0.01
ferricytochrome b5
mutant Y93H, pH 7.0, 25°C
0.011
ferricytochrome b5
-
recombinant enzyme
0.011
ferricytochrome b5
mutant Y93F, pH 7.0, 25°C
0.011
ferricytochrome b5
mutant Y93W, pH 7.0, 25°C
0.012
ferricytochrome b5
mutant P92G, pH 7.0, 25°C
0.012
ferricytochrome b5
mutant P92S, pH 7.0, 25°C
0.012
ferricytochrome b5
mutant Y93S, pH 7.0, 25°C
0.013
ferricytochrome b5
wild-type, pH 7.0, 25°C
0.013
ferricytochrome b5
-
pH 7.0, wild type enzyme
0.014
ferricytochrome b5
-
pH 7.0, S127P mutant enzyme
0.014
ferricytochrome b5
mutant Y93A, pH 7.0, 25°C
0.015
ferricytochrome b5
mutant P92A, pH 7.0, 25°C
0.001
ferrocytochrome b5
mutant G179P, pH 7.0
0.008
ferrocytochrome b5
mutant G179A, pH 7.0
0.013
ferrocytochrome b5
wild-type, pH 7.0
0.043
ferrocytochrome b5
mutant G179T, pH 7.0
0.107
ferrocytochrome b5
mutant G179V, pH 7.0
0.003
NADH
F251Y mutant enzyme, pH 7.0, 25°C
0.003
NADH
-
pH 7.0, wild type enzyme with cytochrome b5 as substrate
0.0038
NADH
mutant Y93S, pH 7.0, 25°C
0.0048
NADH
mutant P92A, pH 7.0, 25°C
0.0049
NADH
mutant Y93D, pH 7.0, 25°C
0.005
NADH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
0.006
NADH
-
recombinant enzyme
0.006
NADH
wild-type, pH 7.0
0.006
NADH
wild-type, pH 7.0, 25°C
0.006
NADH
D239E mutant enzyme, pH 7.0, 25°C
0.006
NADH
-
pH 7.0, wild type enzyme with ferricyanide as substrate
0.006
NADH
wild type enzyme, pH 7.0, 25°C
0.0065
NADH
mutant P92G, pH 7.0, 25°C
0.0067
NADH
mutant Y93F, pH 7.0, 25°C
0.0073
NADH
mutant Y93A, pH 7.0, 25°C
0.0077
NADH
mutant P92S, pH 7.0, 25°C
0.0088
NADH
mutant Y93H, pH 7.0, 25°C
0.012
NADH
F251R mutant enzyme, pH 7.0, 25°C
0.017
NADH
D239S mutant enzyme, pH 7.0, 25°C
0.025
NADH
-
pH 7.0, S127P mutant enzyme with cytochrome b5 as substrate
0.025
NADH
mutant G179A, pH 7.0
0.054
NADH
mutant Y93W, pH 7.0, 25°C
0.055
NADH
-
pH 7.0, S127P mutant enzyme with ferricyanide as substrate
0.119
NADH
D239T mutant enzyme, pH 7.0, 25°C
0.224
NADH
D239S/F251R mutant enzyme, pH 7.0, 25°C
0.512
NADH
D239T/F251R mutant enzyme, pH 7.0, 25°C
0.595
NADH
mutant G179P, pH 7.0
0.662
NADH
mutant G179T, pH 7.0
1.077
NADH
mutant G179V, pH 7.0
0.001
NADPH
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.009
NADPH
D239T mutant enzyme, pH 7.0, 25°C
0.022
NADPH
D239S/F251R mutant enzyme, pH 7.0, 25°C
0.025
NADPH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
0.044
NADPH
D239T/F251R mutant enzyme, pH 7.0, 25°C
0.094
NADPH
D239E mutant enzyme, pH 7.0, 25°C
0.138
NADPH
F251R mutant enzyme, pH 7.0, 25°C
0.268
NADPH
D239S mutant enzyme, pH 7.0, 25°C
0.375
NADPH
mutant G179V, pH 7.0
0.507
NADPH
mutant G179T, pH 7.0
0.617
NADPH
F251Y mutant enzyme, pH 7.0, 25°C
0.924
NADPH
wild-type, pH 7.0
0.924
NADPH
wild type enzyme, pH 7.0, 25°C
1.36
NADPH
mutant G179A, pH 7.0
2.317
NADPH
mutant G179P, pH 7.0
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33 - 417
ferricytochome b5
-
1 - 400
ferricytochrome b5
10 - 400
ferrocytochrome b5
12
ferricyanide
mutant G179V, pH 7.0
21.7
ferricyanide
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
33
ferricyanide
mutant G179T, pH 7.0
40
ferricyanide
K110Q mutant enzyme
42
ferricyanide
mutant G179P, pH 7.0
83
ferricyanide
mutant Y93D, pH 7.0, 25°C
83
ferricyanide
mutant Y93H, pH 7.0, 25°C
83
ferricyanide
mutant Y93W, pH 7.0, 25°C
100
ferricyanide
P144L/L148P mutant enzyme, pH 7.0, 25°C
120
ferricyanide
K110E mutant enzyme
133
ferricyanide
mutant Y93S, pH 7.0, 25°C
200
ferricyanide
mutant Y93A, pH 7.0, 25°C
270
ferricyanide
K110A mutant enzyme
283
ferricyanide
P144L mutant enzyme, pH 7.0, 25°C
300
ferricyanide
L148P mutant enzyme, pH 7.0, 25°C
300
ferricyanide
-
pH 7.0, S127P mutant enzyme
340
ferricyanide
K110H mutant enzyme
467
ferricyanide
mutant P92G, pH 7.0, 25°C
470
ferricyanide
K110R mutant enzyme
483
ferricyanide
mutant Y93F, pH 7.0, 25°C
517
ferricyanide
mutant P92A, pH 7.0, 25°C
559
ferricyanide
mutant G179A, pH 7.0
800
ferricyanide
recombinant wild-type enzyme
800
ferricyanide
wild-type, pH 7.0, 25°C
800
ferricyanide
-
pH 7.0, wild type enzyme
800
ferricyanide
wild type enzyme, pH 7.0, 25°C
800
ferricyanide
wild-type, pH 7.0
880
ferricyanide
mutant P92S, pH 7.0, 25°C
33
ferricytochome b5
P144L/L148P mutant enzyme, pH 7.0, 25°C
-
117
ferricytochome b5
P144L mutant enzyme, pH 7.0, 25°C
-
130
ferricytochome b5
L148P mutant enzyme, pH 7.0, 25°C
-
417
ferricytochome b5
wild type enzyme, pH 7.0, 25°C
-
1
ferricytochrome b5
K110E mutant enzyme
4
ferricytochrome b5
K110Q mutant enzyme
8.3
ferricytochrome b5
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
14
ferricytochrome b5
mutant Y93D, pH 7.0, 25°C
19
ferricytochrome b5
mutant Y93W, pH 7.0, 25°C
27
ferricytochrome b5
mutant Y93H, pH 7.0, 25°C
32
ferricytochrome b5
mutant Y93S, pH 7.0, 25°C
57
ferricytochrome b5
mutant Y93A, pH 7.0, 25°C
90
ferricytochrome b5
K110A mutant enzyme
106
ferricytochrome b5
-
pH 7.0, S127P mutant enzyme
110
ferricytochrome b5
K110H mutant enzyme
200
ferricytochrome b5
K110R mutant enzyme
270
ferricytochrome b5
recombinant wild-type enzyme
295
ferricytochrome b5
mutant Y93F, pH 7.0, 25°C
315
ferricytochrome b5
mutant P92S, pH 7.0, 25°C
320
ferricytochrome b5
mutant P92A, pH 7.0, 25°C
335
ferricytochrome b5
mutant P92G, pH 7.0, 25°C
367
ferricytochrome b5
-
pH 7.0, wild type enzyme
400
ferricytochrome b5
wild-type, pH 7.0, 25°C
10
ferrocytochrome b5
mutant G179P, pH 7.0
17
ferrocytochrome b5
mutant G179V, pH 7.0
18
ferrocytochrome b5
mutant G179T, pH 7.0
245
ferrocytochrome b5
mutant G179A, pH 7.0
400
ferrocytochrome b5
wild-type, pH 7.0
250
NADH
D239S/F251R mutant enzyme, pH 7.0, 25°C
333
NADH
D239T mutant enzyme, pH 7.0, 25°C
367
NADH
F251Y mutant enzyme, pH 7.0, 25°C
433
NADH
D239S mutant enzyme, pH 7.0, 25°C
467
NADH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
500
NADH
F251R mutant enzyme, pH 7.0, 25°C
517
NADH
D239E mutant enzyme, pH 7.0, 25°C
717
NADH
D239T/F251R mutant enzyme, pH 7.0, 25°C
800
NADH
wild type enzyme, pH 7.0, 25°C
5.2
NADPH
D239E mutant enzyme, pH 7.0, 25°C
8
NADPH
mutant G179V, pH 7.0
12
NADPH
mutant G179T, pH 7.0
17
NADPH
mutant G179P, pH 7.0
33
NADPH
wild type enzyme, pH 7.0, 25°C
33
NADPH
wild-type, pH 7.0
48
NADPH
mutant G179A, pH 7.0
50
NADPH
F251R mutant enzyme, pH 7.0, 25°C
50
NADPH
F251Y mutant enzyme, pH 7.0, 25°C
200
NADPH
D239S/F251R mutant enzyme, pH 7.0, 25°C
217
NADPH
D239S mutant enzyme, pH 7.0, 25°C
267
NADPH
D239T mutant enzyme, pH 7.0, 25°C
417
NADPH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
550
NADPH
D239T/F251R mutant enzyme, pH 7.0, 25°C
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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
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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
brenda
Borgese, N.; Pietrini, G.
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Oryctolagus cuniculus, Rattus norvegicus
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Rattus norvegicus
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Rattus norvegicus
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Rattus norvegicus (P20070)
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Rattus norvegicus
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Rattus norvegicus (P20070)
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Rattus norvegicus (P20070)
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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
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42
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2003
Rattus norvegicus
brenda
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
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Mus musculus (Q3TDX8), Mus musculus, Rattus norvegicus (Q68EJ0)
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44
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2005
Rattus norvegicus (P20070)
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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
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44
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2005
Rattus norvegicus (P20070)
brenda
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Rattus norvegicus
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Homo sapiens (P00387), Homo sapiens, Rattus norvegicus (P20070)
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Molecular dynamics simulation study on stabilities and reactivities of NADH cytochrome B5 reductase
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Rattus norvegicus (P20070)
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Yantsevich, A.V.; Gilep, A.A.; Usanov, S.A.
Mechanism of electron transfer in fusion protein cytochrome b5-NADH-cytochrome b5 reductase
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2008
Rattus norvegicus
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Samhan-Arias, A.K.; Garcia-Bereguiain, M.A.; Martin-Romero, F.J.; Gutierrez-Merino, C.
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2009
Rattus norvegicus (P20070)
brenda
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
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2010
Rattus norvegicus
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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
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Rattus norvegicus
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brenda
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
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1325-1334
2016
Rattus norvegicus
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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.
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Rattus norvegicus
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Nikiforova, A.B.; Saris, N.E.; Kruglov, A.G.
External mitochondrial NADH-dependent reductase of redox cyclers VDAC1 or Cyb5R3?
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Rattus norvegicus
brenda
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
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Rattus norvegicus
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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
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109-114
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Homo sapiens, Rattus norvegicus
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