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1 tion pathways draw on reducing power held by NADPH-cytochrome P450 reductase.
2 site conformations that cannot be reduced by NADPH-cytochrome P450 reductase.
3  cytochrome b5 and a 10-fold molar excess of NADPH-cytochrome P450 reductase.
4 two electrons delivered by the FMN domain of NADPH-cytochrome P450 reductase.
5 the presence of molecular oxygen, NADPH, and NADPH-cytochrome P450 reductase.
6 1 is also mutually exclusive with binding of NADPH-cytochrome P450 reductase.
7 nditions by the one-electron reducing enzyme NADPH:cytochrome P450 reductase.
8 nd FMN-containing flavoprotein homologous to NADPH: cytochrome P450 reductase.
9 of an enzymatic assay specific for FMN-bound NADPH cytochrome P450 reductase activity in the absence
10  This treatment also results in increases in NADPH cytochrome P450 reductase and P-glycoprotein (the
11  reduction of oxygen by flavoenzymes such as NADPH-cytochrome P450 reductase and mitochondrial NADH d
12                              The enzyme uses NADPH-cytochrome P450 reductase as a donor of electrons
13 s establish that reduction of the mutants by NADPH-cytochrome P450 reductase, as observed, is thermod
14 utathione synthetase, glutathione reductase, NADPH-cytochrome P450 reductase, biliverdin reductase, a
15  interactions were altered, and the putative NADPH-cytochrome P450 reductase binding site was reforme
16                                              NADPH cytochrome P450 reductase binds two flavin cofacto
17             The reductase domain, similar to NADPH-cytochrome P450 reductase, can be further divided
18                     Availability of a stable NADPH-cytochrome P450 reductase capable of donating only
19 -pong mechanism previously described for the NADPH-cytochrome P450 reductase-catalyzed reduction of c
20 enine dinucleotide phosphate (reduced form) (NADPH)-cytochrome P450 reductase cDNAs is also reported.
21 bolic resistance to insecticides and require NADPH cytochrome P450 reductase (CPR) to transfer electr
22 ecessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free ir
23                                         When NADPH-cytochrome P450 reductase (CPR) and a single P450
24 e P450 (heme-binding) catalytic domain and a NADPH-cytochrome P450 reductase (CPR) domain containing
25 se model with liver-specific deletion of the NADPH-cytochrome P450 reductase (Cpr) gene (designated A
26 odel that has liver-specific deletion of the NADPH-cytochrome P450 reductase (Cpr) gene.
27                                              NADPH-cytochrome P450 reductase (CPR) is an essential co
28                   In this study we show that NADPH-cytochrome P450 reductase (CPR) is capable of supp
29                                   Microsomal NADPH-cytochrome P450 reductase (CPR) is one of only two
30                                              NADPH-cytochrome P450 reductase (CPR), a diflavin reduct
31  conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomai
32 NOS) flavin domains closely resemble that of NADPH-cytochrome P450 reductase (CPR), with the exceptio
33 talytic function requiring interactions with NADPH-cytochrome P450 reductase (CPR).
34 hase flavin domains closely resemble that of NADPH-cytochrome P450 reductase (CPR).
35 d for mixed reconstituted systems containing NADPH-cytochrome P450 reductase, CYP2B4, and CYP1A2, whe
36                     The crystal structure of NADPH-cytochrome P450 reductase (CYPOR) implies that a l
37 cking the essential cofactor of Cyp enzymes, NADPH-cytochrome p450 reductase (Cypor), were selected i
38        In a reconstituted system with insect NADPH cytochrome P450 reductase, cytochrome b5, and NADP
39                                              NADPH-cytochrome P450 reductase delivers electrons requi
40  Heme oxygenase (HO) catalyzes the O(2)- and NADPH-cytochrome P450 reductase-dependent conversion of
41 Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of h
42 tants investigated, only G139A catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of h
43 ndividually does not significantly alter the NADPH-cytochrome P450 reductase-dependent reaction regio
44 n protein constructed of cytochrome P450 and NADPH-cytochrome P450 reductase domains.
45 HT in transgenic mice carrying a hypomorphic NADPH-cytochrome P450 reductase gene (Cpr-low mice).
46 esoheme by human truncated HO-1 supported by NADPH-cytochrome P450 reductase, H2O2, or ascorbate have
47  knockdown of endoplasmic reticulum cofactor NADPH-cytochrome P450 reductase had no effect, while kno
48 ) form of the reductase, the T491V mutant of NADPH-cytochrome P450 reductase has been reconstituted w
49                                              NADPH-cytochrome P450 reductase is a flavoprotein which
50                                              NADPH-cytochrome P450 reductase is a multi-domain redox
51 ion of HO-1, biliverdin reductase (BVR), and NADPH:cytochrome P450 reductase (NPR) in pulmonary arter
52 pressing NADH:cytochrome b5 reductase (NBR), NADPH:cytochrome P450 reductase (NPR), or NADPH: quinone
53 as CO, a reaction supported by both H2O2 and NADPH-cytochrome P450 reductase/O2.
54 xidize heme in reactions supported by either NADPH-cytochrome P450 reductase or ascorbic acid has bee
55 6, 2B1, 2C9, 2C9 C175R, 3A4, 3A4-HT) and rat NADPH cytochrome P450 reductase (P450 reductase).
56 chrome P450 monooxygenase system consists of NADPH-cytochrome P450 reductase (P450 reductase) and cyt
57 omes P450 requires the membrane-bound enzyme NADPH-cytochrome P450 reductase (P450 reductase), which
58  NADPH/FAD binding domains, respectively) of NADPH-cytochrome P450 reductases (P450 reductases), thes
59 [triiodothyronine (T3)] positively regulates NADPH cytochrome P450 reductase (P450R) mRNA expression
60 man CYP2B6) is delivered in combination with NADPH-cytochrome P450 reductase (P450R), which encodes t
61                               In particular, NADPH:cytochrome P450 reductase (P450R) plays a major ro
62                                              NADPH-cytochrome P450 reductase (POR) is essential for t
63 bound enzymes that rely on the same protein, NADPH-cytochrome P450 reductase (POR), to provide the el
64 me circumstances, also accept electrons from NADPH:cytochrome P450 reductase, potentially allowing fo
65 ) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron,
66             Here we report that FAC binds to NADPH cytochrome-P450 reductase (RED), a microsomal memb
67 cted RNAi knock-down of Drosophila CYP4G1 or NADPH-cytochrome P450 reductase results in flies deficie
68            Catalytic turnover of CYP4F4 with NADPH-cytochrome P450 reductase shows that the heme is c
69    In the presence of ascorbate or the human NADPH cytochrome P450 reductase system, the heme-HemO co
70 1F mutant when these proteins are reduced by NADPH-cytochrome P450 reductase than by dithionite.
71 n of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for
72 ol ring structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron.
73 nstituted enzyme system containing NADPH and NADPH-cytochrome P450 reductase under aerobic conditions