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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 ochrome P450 oxidoreductase or mitochondrial adrenodoxin.
5 The purified P450MT2 showed a preference for adrenodoxin + adrenodoxin reductase electron donor syste
11 ystal structure of the homologous ferredoxin adrenodoxin (Adx) and loose restraints determined from p
12 e vertebrate-type ferredoxins, the mammalian adrenodoxin (Adx) and the bacterial ferredoxins putidare
14 Co-expression with wild type P4501A1 and adrenodoxin (Adx) cDNAs resulted in 5-7-fold higher eryt
16 and spectral studies show that the wild-type adrenodoxin (Adx), but not the mutant Adx, binds to P450
17 o mitochondria (P450MT2) which interact with adrenodoxin (Adx), cytochrome P450 reductase (CPR) and b
20 responsible for its observed preference for adrenodoxin and adrenodoxin reductase electron transfer
21 g recombinant human CYP11B2 as well as human adrenodoxin and adrenodoxin reductase was established to
23 450 2D6 (CYP2D6), supported by mitochondrial adrenodoxin and adrenodoxin reductase, can efficiently c
26 YP1B1 supported by mitochondrial ferredoxin (adrenodoxin) and ferredoxin reductase showed high aryl h
28 tructure contains a large dipole moment like adrenodoxin, and appears to have a similar interaction d
29 reconstituted with the iron-sulfer protein, adrenodoxin, and the flavoprotein, adrenodoxin reductase
31 results in virtually complete inhibition of adrenodoxin binding, in P450c27 there are three of such
32 s of the approximately 30-fold difference in adrenodoxin binding, two sets of P450c27 mutants were ge
35 utations of one set were within the putative adrenodoxin-binding site containing conserved lysine res
36 ximately 20-fold increase in apparent Ks for adrenodoxin, confirming that these two positively charge
37 posed of 105 residues with similarity to the adrenodoxin family of [2Fe-2S] bacterial ferredoxins.
40 n ferredoxin, the human equivalent of bovine adrenodoxin, is a small iron-sulfur protein with one [2F
41 multiple ancient connections between Fe2S2- (adrenodoxin-like) and heme- (cytochrome c) binding domai
42 fer is a shared mechanistic feature with the adrenodoxin P450 and photosynthetic electron-transfer sy
44 ximal surface identifies the determinants of adrenodoxin recognition as a constellation of conserved
45 e intensively studied monoflavin reductases, adrenodoxin reductase (AdR) and ferredoxin-NADP+ reducta
50 450MT2 showed a preference for adrenodoxin + adrenodoxin reductase electron donor system and exhibite
53 man CYP11B2 as well as human adrenodoxin and adrenodoxin reductase was established to help maximize t
55 protein, adrenodoxin, and the flavoprotein, adrenodoxin reductase, and show the NADPH and time-depen
56 concert with its cofactors, adrenodoxin and adrenodoxin reductase, and the transcription factor ster
57 , supported by mitochondrial adrenodoxin and adrenodoxin reductase, can efficiently catalyze the meta
64 higher affinity for the common redox partner adrenodoxin than another mitochondrial P450, P450scc (pr
65 oteins, CsmI, CsmJ, and CsmX, are related to adrenodoxin-type ferredoxins that ligate [2Fe-2S] cluste
68 n the oxidized (Adx(o)) and reduced (Adx(r)) adrenodoxin were probed by measurement of (15)N relaxati
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