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

1 o membrane interactions and interaction with cytochrome P450 reductase.

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

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

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

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

6 containing flavoprotein homologous to NADPH: cytochrome P450 reductase.

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

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

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

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

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

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

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

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

15 127, and Glu190 contribute to the binding of 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 The enzyme uses NADPH-cytochrome P450 reductase as a donor of electrons and hy

30 A1) in Selaginella relies on NADPH-dependent cytochrome P450 reductase as sole redox partner, distinc

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

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

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

34 NADPH cytochrome P450 reductase binds two flavin cofactors, FM

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

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

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

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

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

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

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

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

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

44 0MT2) which interact with adrenodoxin (Adx), cytochrome P450 reductase (CPR) and bacterial flavodoxin

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

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

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

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

49 (heme-binding) catalytic domain and a NADPH-cytochrome P450 reductase (CPR) domain containing FAD an

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

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

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

53 450 (P450 or CYP for a specific isoform) and cytochrome P450 reductase (CPR) has been generally accep

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

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

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

57 onic cytochrome P450 (CYP450) and an anionic cytochrome P450 reductase (CPR) in non-ionic inulin-base

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

59 Plant NADPH-dependent cytochrome P450 reductase (CPR) is a multidomain enzyme

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

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

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

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

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

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

66 me b5 (B5)/cytochrome b5 reductase (B5R) and cytochrome P450 reductase (CPR) were measured in aortic

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

86 selectively expand hepatocytes deficient in cytochrome p450 reductase (Cypor) using acetaminophen (A

87 the essential cofactor of Cyp enzymes, NADPH-cytochrome p450 reductase (Cypor), were selected in vivo

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

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

90 NADPH-cytochrome P450 reductase delivers electrons required by

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

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

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

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

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

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

97 ein constructed of cytochrome P450 and NADPH-cytochrome P450 reductase domains.

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

99 nes encoding known redox partners for P450s (cytochrome P450 reductase, ferredoxin and ferredoxin red

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

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

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

103 down of endoplasmic reticulum cofactor NADPH-cytochrome P450 reductase had no effect, while knockdown

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

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

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

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

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

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

110 NADPH-cytochrome P450 reductase is a flavoprotein which contai

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

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

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

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

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

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

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

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

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

120 450 requires the membrane-bound enzyme NADPH-cytochrome P450 reductase (P450 reductase), which transf

121 , 2C9, 2C9 C175R, 3A4, 3A4-HT) and rat NADPH cytochrome P450 reductase (P450 reductase).

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

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

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

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

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

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

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

129 enzymes that rely on the same protein, NADPH-cytochrome P450 reductase (POR), to provide the electron

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

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

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

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

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

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

136 Cytochrome P450 reductase reduces the unmodified and tBP

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

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

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

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

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

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

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

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

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

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

147 Unlike cytochrome P450 reductase, the switch in coenzyme specif

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

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

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

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

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

153 Cytochrome P450 reductase, which delivers electrons from