ライフサイエンスコーパス: cytochrome P450 reductase

1 , were shown to exhibit decreased binding to cytochrome P450 reductase.

2 hrome b5 and a 10-fold molar excess of NADPH-cytochrome P450 reductase.

3 esence of molecular oxygen, NADPH, and NADPH-cytochrome P450 reductase.

4 containing flavoprotein homologous to NADPH: cytochrome P450 reductase.

5 lso mutually exclusive with binding of NADPH-cytochrome P450 reductase.

6 ns by the one-electron reducing enzyme NADPH:cytochrome P450 reductase.

7 cludes its reduction with the redox partner, cytochrome P450 reductase.

8 o likely to apply to related enzymes such as cytochrome P450 reductase.

9 noticeable modulation due to the presence of cytochrome P450 reductase.

10 l) when supplemented with even low levels of cytochrome P450 reductase.

11 athways draw on reducing power held by NADPH-cytochrome P450 reductase.

12 ectrons delivered by the FMN domain of NADPH-cytochrome P450 reductase.

13 onformations that cannot be reduced by NADPH-cytochrome P450 reductase.

14 127, and Glu190 contribute to the binding of cytochrome P450 reductase.

15 o membrane interactions and interaction with cytochrome P450 reductase.

16 This is replaced by Trp676 in human cytochrome P450 reductase, a tryptophan in related difla

17 profiles were confirmed using purified human cytochrome P450 reductase, acidic activation, and UV-Vis

18 enzymatic assay specific for FMN-bound NADPH cytochrome P450 reductase activity in the absence of its

19 PH of the FAD and FMN redox centers in human cytochrome P450 reductase and its component domains has

20 tion of oxygen by flavoenzymes such as NADPH-cytochrome P450 reductase and mitochondrial NADH dehydro

21 th reduction of the iron and the presence of cytochrome P450 reductase and NADPH.

22 cubations were carried out in the absence of cytochrome P450 reductase and NADPH.

23 ts the one-electron reduction of quinones by cytochrome P450 reductase and other flavoproteins that w

24 treatment also results in increases in NADPH cytochrome P450 reductase and P-glycoprotein (the MDR1 g

25 In addition, purified microsomal cytochrome P450 reductase and soluble cytochrome b5 reco

26 found that CYP2S1 was not readily reduced by cytochrome P450 reductase, and thus no activity was foun

27 that the binding sites for cytochrome b5 and cytochrome P450 reductase are, as predicted, located on

28 f NADPH, and coupling with its redox partner cytochrome P450 reductase, aromatase converts androstene

29 blish that reduction of the mutants by NADPH-cytochrome P450 reductase, as observed, is thermodynamic

30 one synthetase, glutathione reductase, NADPH-cytochrome P450 reductase, biliverdin reductase, and thi

31 actions were altered, and the putative NADPH-cytochrome P450 reductase binding site was reformed.

32 NADPH cytochrome P450 reductase binds two flavin cofactors, FM

33 ts redox partners: cytochrome b5 (cytb5) and cytochrome P450 reductase, both of which are membrane pr

34 omplexes are reduced to the ferrous state by cytochrome P450 reductase but do not catalyze alpha-meso

35 P27 fusion protein can be reconstituted with cytochrome P450 reductase, but the mitochondrial associa

36 The reductase domain, similar to NADPH-cytochrome P450 reductase, can be further divided into t

37 Availability of a stable NADPH-cytochrome P450 reductase capable of donating only a sin

38 diflavin reductases exemplified by mammalian cytochrome P450 reductase catalyze NADPH dehydrogenation

39 mechanism previously described for the NADPH-cytochrome P450 reductase-catalyzed reduction of cytochr

40 inucleotide phosphate (reduced form) (NADPH)-cytochrome P450 reductase cDNAs is also reported.

41 When NADPH-cytochrome P450 reductase (CPR) and a single P450 were i

42 0MT2) which interact with adrenodoxin (Adx), cytochrome P450 reductase (CPR) and bacterial flavodoxin

43 Mammalian cytochrome P450 reductase (CPR) and cytochrome P450 (CP)

44 thermodynamics of coenzyme binding to human cytochrome P450 reductase (CPR) and its isolated FAD-bin

45 active site structure induced by binding of cytochrome P450 reductase (CPR) and Mn(III) cytochrome b

46 The redox properties of human cytochrome P450 reductase (CPR) are similar to those rep

47 CYP51 and cytochrome P450 reductase (CPR) from TB were cloned, exp

48 el with liver-specific deletion of the NADPH-cytochrome P450 reductase (Cpr) gene (designated Alb-Cre

49 hat has liver-specific deletion of the NADPH-cytochrome P450 reductase (Cpr) gene.

50 450 (P450 or CYP for a specific isoform) and cytochrome P450 reductase (CPR) has been generally accep

51 ating interflavin electron transfer in human cytochrome P450 reductase (CPR) has been studied using t

52 nd CYP6AA7 were separately co-expressed with cytochrome P450 reductase (CPR) in insect Spodoptera fru

53 by another redox active protein, for example cytochrome P450 reductase (CPR) in mammalian endoplasmic

54 Cytochrome P450 reductase (CPR) is a diflavin enzyme tha

55 Cytochrome P450 reductase (CPR) is a tethered membrane p

56 NADPH-cytochrome P450 reductase (CPR) is an essential componen

57 In this study we show that NADPH-cytochrome P450 reductase (CPR) is capable of supporting

58 Microsomal NADPH-cytochrome P450 reductase (CPR) is one of only two mamma

59 Cytochrome P450 reductase (CPR) is the redox partner for

60 resistance to insecticides and require NADPH cytochrome P450 reductase (CPR) to transfer electrons wh

61 NADPH-cytochrome P450 reductase (CPR), a diflavin reductase, p

62 the diradical (disemiquinoid) form of human cytochrome P450 reductase (CPR), a nicotinamide adenine

63 rmational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redo

64 ource of electrons and an additional enzyme, cytochrome P450 reductase (CPR), as the electron transfe

65 heir electron transferring protein partners, cytochrome P450 reductase (CPR), ferredoxin reductase (F

66 veral reductants, including ascorbate, yeast cytochrome P450 reductase (CPR), human CPR, spinach ferr

67 ry for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free iron and

68 lavin domains closely resemble that of NADPH-cytochrome P450 reductase (CPR), with the exception of a

69 lavin domains closely resemble that of NADPH-cytochrome P450 reductase (CPR).

70 iron with electrons delivered from NADPH via cytochrome P450 reductase (CPR).

71 c function requiring interactions with NADPH-cytochrome P450 reductase (CPR).

72 and binding energy propagation through human cytochrome P450 reductase (CPR).

73 e P450s and their cognate redox partner, the cytochrome P450 reductase (CPR).

74 ctron donor to all microsomal P450 proteins, cytochrome P450 reductase (Cpr).

75 dependent diflavin oxidoreductase related to cytochrome P450 reductase (CPR).

76 Cytochrome P450-reductase (CPR) is a versatile NADPH-dep

77 rotein, NADH:ferrihemoprotein reductase (EC, cytochrome P450 reductase, CPR) in the liver, resulting

78 mixed reconstituted systems containing NADPH-cytochrome P450 reductase, CYP2B4, and CYP1A2, where a d

79 The crystal structure of NADPH-cytochrome P450 reductase (CYPOR) implies that a large d

80 In a reconstituted system with insect NADPH cytochrome P450 reductase, cytochrome b5, and NADPH, the

81 poxidation when reconstituted with house fly cytochrome P450 reductase, cytochrome P450 6A1, phosphol

82 oxygenase (HO) catalyzes the O(2)- and NADPH-cytochrome P450 reductase-dependent conversion of heme t

83 investigated, only G139A catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to

84 heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to

85 ually does not significantly alter the NADPH-cytochrome P450 reductase-dependent reaction regiochemis

86 larity to mammalian P450s, and presence of a cytochrome P450 reductase domain that allows the enzyme

87 P450 cytochrome that is naturally fused to a cytochrome P450 reductase domain.

88 nfer that the flavodoxin-like domains of the cytochrome P450 reductase family form mutually exclusive

89 ome b5, for human steroidogenic CYP17A1, the cytochrome P450 reductase FMN domain delivers both elect

90 transgenic mice carrying a hypomorphic NADPH-cytochrome P450 reductase gene (Cpr-low mice).

91 e by human truncated HO-1 supported by NADPH-cytochrome P450 reductase, H2O2, or ascorbate have been

92 of the reductase, the T491V mutant of NADPH-cytochrome P450 reductase has been reconstituted with 5'

93 The use of 5-deazaFAD T491V cytochrome P450 reductase has made it possible to direct

94 lavin reduction in two mutant forms of human cytochrome P450 reductase have been studied by stopped-f

95 etics of internal electron transfer in human cytochrome P450 reductase have been studied using temper

96 The cytochrome b5 is reduced by house fly cytochrome P450 reductase in a reconstituted system at a

97 Results from studies on the incorporation of cytochrome P450 reductase into the brain microsomal syst

98 NADPH-cytochrome P450 reductase is a flavoprotein which contai

99 NADPH-cytochrome P450 reductase is a multi-domain redox enzyme

100 Trp676 in human cytochrome P450 reductase is conformationally mobile, an

101 components of the multidomain flavoproteins cytochrome P450 reductase, nitric oxide synthase, and me

102 HO-1, biliverdin reductase (BVR), and NADPH:cytochrome P450 reductase (NPR) in pulmonary artery endo

103 ng NADH:cytochrome b5 reductase (NBR), NADPH:cytochrome P450 reductase (NPR), or NADPH: quinone oxido

104 e employed a powerful new model, the Hepatic Cytochrome P450 Reductase Null (HRN) mouse, which has al

105 a reaction supported by both H2O2 and NADPH-cytochrome P450 reductase/O2.

106 heme in reactions supported by either NADPH-cytochrome P450 reductase or ascorbic acid has been comp

107 P450 monooxygenase system consists of NADPH-cytochrome P450 reductase (P450 reductase) and cytochrom

108 450 requires the membrane-bound enzyme NADPH-cytochrome P450 reductase (P450 reductase), which transf

109 , 2C9, 2C9 C175R, 3A4, 3A4-HT) and rat NADPH cytochrome P450 reductase (P450 reductase).

110 /FAD binding domains, respectively) of NADPH-cytochrome P450 reductases (P450 reductases), these bact

111 dothyronine (T3)] positively regulates NADPH cytochrome P450 reductase (P450R) mRNA expression in rat

112 In particular, NADPH:cytochrome P450 reductase (P450R) plays a major role in

113 mes such as cytochrome b(5) reductase (b5R), cytochrome P450 reductase (P450R), dihydronicotinamide r

114 P2B6) is delivered in combination with NADPH-cytochrome P450 reductase (P450R), which encodes the fla

115 NADPH-cytochrome P450 reductase (POR) is essential for the fun

116 mechanism of action of the membrane-anchored cytochrome P450 reductase (POR) is studied here.

117 reductases is unknown, with the exception of cytochrome P450 reductase (POR).

118 cumstances, also accept electrons from NADPH:cytochrome P450 reductase, potentially allowing for redu

119 ting the molar ratios of cytochrome b(5) and cytochrome P450 reductase present in the incubation mixt

120 ade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, a

121 suitable electron donor, e.g., ascorbate or cytochrome P450 reductase, promotes catalytic degradatio

122 Here we report that FAC binds to NADPH cytochrome-P450 reductase (RED), a microsomal membrane p

123 Cytochrome P450 reductase reduces the unmodified and tBP

124 NAi knock-down of Drosophila CYP4G1 or NADPH-cytochrome P450 reductase results in flies deficient in

125 Catalytic turnover of CYP4F4 with NADPH-cytochrome P450 reductase shows that the heme is covalen

126 complex of cytochrome P450 3A4 (CYP3A4) and cytochrome P450 reductase solubilized via self-assembly

127 the presence of ascorbate or the human NADPH cytochrome P450 reductase system, the heme-HemO complex

128 nctioned as type I nitroreductase (TbNTR) or cytochrome P450 reductase (TbCPR) dependent prodrugs tha

129 ant when these proteins are reduced by NADPH-cytochrome P450 reductase than by dithionite.

130 In NOS and microsomal cytochrome P450 reductase the sq/hq redox potential is l

131 er in the presence or absence of recombinant cytochrome P450 reductase, the cellular level of the CYP

132 O1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, t

133 the electron transfer mechanism of mammalian cytochrome P450 reductase, the FMN semiquinone state is

134 Unlike cytochrome P450 reductase, the switch in coenzyme specif

135 g structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron.

136 ted enzyme system containing NADPH and NADPH-cytochrome P450 reductase under aerobic conditions in a

137 g446 on CYP3A4 in binding to cyt b(5) and/or cytochrome P450 reductase was also discovered.

138 ide anion catalyzed by mtNOS and recombinant cytochrome P450 reductase were consistent with the seque

139 The nNOS reductase domain is homologous to cytochrome P450 reductase, which contains two conserved

140 Cytochrome P450 reductase, which delivers electrons from