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1 lian counterparts, adrenodoxin reductase and adrenodoxin.
2 residues also crucial in P450scc for binding adrenodoxin.
3 rate ferredoxin family which includes bovine adrenodoxin.
4 oth enzymes require the common redox partner adrenodoxin.
5 ng mechanisms in the absence and presence of adrenodoxin.
6 ectrons delivered by the iron/sulfur protein adrenodoxin.
7 argeting the interaction between CYP11B2 and adrenodoxin.
8 ochrome P450 oxidoreductase or mitochondrial adrenodoxin.
9 The purified P450MT2 showed a preference for adrenodoxin + adrenodoxin reductase electron donor syste
10 associated fusion protein is functional with adrenodoxin + adrenodoxin reductase.
11 . the genes and proteins for P450scc enzyme, adrenodoxin, adrenodoxin reductase and MLN64.
12  activity of recombinant h-P450cc24 required adrenodoxin, adrenodoxin reductase, and NADPH.
13       It requires electron transfer from the adrenodoxin/adrenodoxin reductase system to catalyze the
14 dentical and very similar to those of bovine adrenodoxin (Adx) and Escherichia coli ferredoxin.
15 ystal structure of the homologous ferredoxin adrenodoxin (Adx) and loose restraints determined from p
16 e vertebrate-type ferredoxins, the mammalian adrenodoxin (Adx) and the bacterial ferredoxins putidare
17                                              Adrenodoxin (Adx) belongs to the family of Cys(4)Fe(2)S(
18     Co-expression with wild type P4501A1 and adrenodoxin (Adx) cDNAs resulted in 5-7-fold higher eryt
19 (cAMP) regulates transcription of the bovine adrenodoxin (Adx) gene in the adrenal cortex.
20 and spectral studies show that the wild-type adrenodoxin (Adx), but not the mutant Adx, binds to P450
21 -protein interactions with the redox partner Adrenodoxin (Adx), but the structural basis of the subst
22 o mitochondria (P450MT2) which interact with adrenodoxin (Adx), cytochrome P450 reductase (CPR) and b
23 oxycholesterol and the protein redox partner adrenodoxin (Adx).
24                                Mitochondrial adrenodoxins (ADXs) are small iron-sulfur proteins with
25 using hydrophobic chromatography followed by adrenodoxin affinity binding.
26                                              Adrenodoxin allosterically modulates CYP11B2 function se
27  responsible for its observed preference for adrenodoxin and adrenodoxin reductase electron transfer
28 g recombinant human CYP11B2 as well as human adrenodoxin and adrenodoxin reductase was established to
29               In concert with its cofactors, adrenodoxin and adrenodoxin reductase, and the transcrip
30 450 2D6 (CYP2D6), supported by mitochondrial adrenodoxin and adrenodoxin reductase, can efficiently c
31 450 2D6 (CYP2D6), supported by mitochondrial adrenodoxin and adrenodoxin reductase, can efficiently c
32 hondrial enzyme was supported exclusively by adrenodoxin and adrenodoxin reductase.
33 icosatetraenoic acid when reconstituted with adrenodoxin and adrenodoxin reductase.
34  isoforms of [2Fe-2S] ferredoxins, FDX1 (aka adrenodoxin) and FDX2, with known functions in cytochrom
35 YP1B1 supported by mitochondrial ferredoxin (adrenodoxin) and ferredoxin reductase showed high aryl h
36 embrane-bound enzymes: aldosterone synthase, adrenodoxin, and adrenodoxin reductase.
37 tructure contains a large dipole moment like adrenodoxin, and appears to have a similar interaction d
38  reconstituted with the iron-sulfer protein, adrenodoxin, and the flavoprotein, adrenodoxin reductase
39 y, to serine also decreased the affinity for adrenodoxin approximately 20-fold.
40  results in virtually complete inhibition of adrenodoxin binding, in P450c27 there are three of such
41 s of the approximately 30-fold difference in adrenodoxin binding, two sets of P450c27 mutants were ge
42 354A/K358A/R418S mutation profoundly reduced adrenodoxin binding.
43 ved in mitochondrial P450s are important for adrenodoxin binding.
44 utations of one set were within the putative adrenodoxin-binding site containing conserved lysine res
45                   Indeed, local increases in adrenodoxin concentration promote binding of the substra
46 ximately 20-fold increase in apparent Ks for adrenodoxin, confirming that these two positively charge
47 about the structural and functional basis of adrenodoxin/CYP11B2 interaction, which impedes the devel
48 posed of 105 residues with similarity to the adrenodoxin family of [2Fe-2S] bacterial ferredoxins.
49                           The electron donor adrenodoxin had little effect on binding; the substrate
50 ture of a closely related ferredoxin, bovine adrenodoxin, has been published.
51        The CYP11B2 structure in complex with adrenodoxin identified specific residues at the protein-
52 ematic study was carried out to determine if adrenodoxin interaction with CYP11B2 might also have an
53 Lys-354, Lys-358, and Arg-418) important for adrenodoxin interaction.
54 , stopped-flow investigations establish that adrenodoxin is also an allosteric modulator of CYP11A1 s
55 n ferredoxin, the human equivalent of bovine adrenodoxin, is a small iron-sulfur protein with one [2F
56 multiple ancient connections between Fe2S2- (adrenodoxin-like) and heme- (cytochrome c) binding domai
57 ces between different P450 interactions with adrenodoxin may provide valuable clues for an orthogonal
58 fer is a shared mechanistic feature with the adrenodoxin P450 and photosynthetic electron-transfer sy
59 minal domains to [2Fe-2S] ferredoxins of the adrenodoxin/putidaredoxin subfamily of ferredoxins.
60 ximal surface identifies the determinants of adrenodoxin recognition as a constellation of conserved
61 e intensively studied monoflavin reductases, adrenodoxin reductase (AdR) and ferredoxin-NADP+ reducta
62 proteins, cytochrome P450 11A1 (CYP11A1) and adrenodoxin reductase (AdR).
63  animals, ADXs transfer electrons between an adrenodoxin reductase (ADXR) and mitochondrial P450s, wh
64 ribe the Drosophila dare gene, which encodes adrenodoxin reductase (AR).
65 dox couple and their mammalian counterparts, adrenodoxin reductase and adrenodoxin.
66 nd proteins for P450scc enzyme, adrenodoxin, adrenodoxin reductase and MLN64.
67 450MT2 showed a preference for adrenodoxin + adrenodoxin reductase electron donor system and exhibite
68  its observed preference for adrenodoxin and adrenodoxin reductase electron transfer proteins.
69        Finally, the expression of Drosophila Adrenodoxin Reductase increases during mid-oogenesis and
70 man CYP11B2 as well as human adrenodoxin and adrenodoxin reductase was established to help maximize t
71 recombinant h-P450cc24 required adrenodoxin, adrenodoxin reductase, and NADPH.
72  protein, adrenodoxin, and the flavoprotein, adrenodoxin reductase, and show the NADPH and time-depen
73  concert with its cofactors, adrenodoxin and adrenodoxin reductase, and the transcription factor ster
74 , supported by mitochondrial adrenodoxin and adrenodoxin reductase, can efficiently catalyze the conv
75 , supported by mitochondrial adrenodoxin and adrenodoxin reductase, can efficiently catalyze the meta
76                         Presence of P450scc, adrenodoxin reductase, cytochrome P450 17-hydroxylase (P
77 was supported exclusively by adrenodoxin and adrenodoxin reductase.
78 ymes: aldosterone synthase, adrenodoxin, and adrenodoxin reductase.
79 ion protein is functional with adrenodoxin + adrenodoxin reductase.
80 acid when reconstituted with adrenodoxin and adrenodoxin reductase.
81                                              Adrenodoxin reduction and hydrogen abstraction both cont
82 a 4-state closed mechanism, while increasing adrenodoxin results in enhancement of the conformational
83  cortisol-producing CYP11B1, which also bind adrenodoxin, revealed substantial structural differences
84 d induced fit mechanism, and the presence of adrenodoxin shifts the mechanism to a 4-state closed mod
85 higher affinity for the common redox partner adrenodoxin than another mitochondrial P450, P450scc (pr
86 ~5-fold stimulatory effect on the binding of adrenodoxin to P450 11A1.
87 oteins, CsmI, CsmJ, and CsmX, are related to adrenodoxin-type ferredoxins that ligate [2Fe-2S] cluste
88                Ferric P450 27C1 reduction by adrenodoxin was 3-fold faster in the presence of the sub
89                                              Adrenodoxin was used as a substitute redox protein and w
90          Oxidized human [2Fe-2S] ferredoxin (adrenodoxin) was used to test the approach.
91 n the oxidized (Adx(o)) and reduced (Adx(r)) adrenodoxin were probed by measurement of (15)N relaxati