ライフサイエンスコーパス: putidaredoxin

1 can be dissociated from electron transfer to putidaredoxin.

2 of diprotein complex formation with reduced putidaredoxin.

3 mphor (23 vs 2 microM) and a poorer K(d) for putidaredoxin (50 vs 20 microM) than wild-type P450(cam)

4 eme active site of the enzyme, although both putidaredoxin and cytochrome b(5) bind to the same or si

5 CYP119 is very slowly reduced by putidaredoxin and putidaredoxin reductase, but these pro

6 ylate lauric acid in a reaction supported by putidaredoxin and putidaredoxin reductase.

7 ygen and reducing equivalents from bacterial putidaredoxin and putidaredoxin reductase.

8 y specific interaction between P450(cam) and putidaredoxin, and that this interaction increases the p

9 pocket environment, such a perturbation upon putidaredoxin binding is suggestive of changes in confor

10 Arg-112, a residue known to be important for putidaredoxin binding, toward the heme.

11 ic structure and/or geometry take place when putidaredoxin binds.

12 x and beta3 and beta5 sheets) and binding of putidaredoxin (C and L helices), the iron-sulfur protein

13 of Pdx, that of the C85S variant of gallium putidaredoxin, in which a nonligand Cys is replaced by S

14 ks at 551 and 561 cm(-1), and the binding of putidaredoxin increases the intensity of the high freque

15 re insensitive to the presence or absence of putidaredoxin, indicating that the geometry of the Fe-X-

16 that the enzyme bound to its redox partner, putidaredoxin, is in a closed state at ambient temperatu

17 Putidaredoxin of the CYP101A1 system from Pseudomonas pu

18 d to identify a part of the binding site for putidaredoxin on an unrelated P450 enzyme.

19 In this study, the effector role of Pdx (putidaredoxin) on cytochrome P450cam conformation is ref

20 Fusion proteins of cytochrome P450cam with putidaredoxin (Pd) and putidaredoxin reductase (PdR), th

21 m (oxy-P450cam) and its complex with reduced putidaredoxin (Pd).

22 enodoxin (Adx) and the bacterial ferredoxins putidaredoxin (Pdx) and terpredoxin (Tdx).

23 alently linked putidaredoxin reductase (Pdr)-putidaredoxin (Pdx) complex.

24 er between putidaredoxin reductase (Pdr) and putidaredoxin (Pdx) from Pseudomonas putida was studied

25 f uniformly 15N-labeled reduced and oxidized putidaredoxin (Pdx) have been studied by 2D 15N NMR rela

26 Putidaredoxin (Pdx) plays an essential role as an electr

27 onooxygenase system from Pseudomonas putida, putidaredoxin (Pdx) shuttles electrons between putidared

28 Pseudomonas putida, the [2Fe-2S]-containing putidaredoxin (Pdx) shuttles electrons between the NADH-

29 (ET) processes from the [2Fe-2S] containing putidaredoxin (Pdx) to P450cam.

30 AM with one equivalent of dithionite-reduced putidaredoxin (Pdx) was monitored for the appearance of

31 ce amino acid residues in the interaction of putidaredoxin (Pdx) with its redox partners in the cytoc

32 ich structures have been determined, Adx and putidaredoxin (Pdx), a homologous Pseudomonas protein.

33 Putidaredoxin (Pdx), a vertebrate-type [2Fe-2S] ferredox

34 plex formed between the [2Fe-2S] ferredoxin, putidaredoxin (Pdx), and cytochrome P450cam (CYP101) fro

35 roteins: NADH-putidaredoxin reductase (Pdr), putidaredoxin (Pdx), and cytochrome P450cam.

36 he open conformation when its redox partner, putidaredoxin (Pdx), binds, whereas recent NMR studies i

37 ural differences in the [2Fe-2S] ferredoxin, putidaredoxin (Pdx), from the camphor hydroxylation path

38 me P450cam complexed with its redox partner, putidaredoxin (Pdx), shows that P450cam adopts the open

39 Stability of the [2Fe-2S]-containing putidaredoxin (Pdx), the electron donor to cytochrome P4

40 ed P450cam complexed with its redox partner, putidaredoxin (Pdx), to 2.2 and 2.09 angstroms, respecti

41 proteins, putidaredoxin reductase (PdR) and putidaredoxin (Pdx), to supply electrons from NADH.

42 CYP101 upon binding of the effector protein putidaredoxin (Pdx).

43 on-transfer steps to the iron-sulfur protein putidaredoxin (Pdx).

44 h are also perturbed by binding of effector, putidaredoxin (Pdx).

45 by the physiological reductant and effector putidaredoxin (Pdx).

46 e perturbed by binding to its redox partner, putidaredoxin (Pdx).

47 al reductant, the Cys(4)Fe(2)S(2) ferredoxin putidaredoxin (Pdx).

48 cam when bound to its natural redox partner, putidaredoxin (Pdx).

49 ole in binding of the P450cam redox partner, putidaredoxin (Pdx).

50 model for the solution structure of oxidized putidaredoxin (Pdxo), a Cys4Fe2S2 ferredoxin, has been d

51 e G248E (but not G248D) mutant with camphor, putidaredoxin, putidaredoxin reductase, and NADH results

52 ppeared to be the recombinant NADH-dependent putidaredoxin/putidaredoxin reductase from Pseudomonas p

53 spinach ferredoxin/ferredoxin reductase, and putidaredoxin/putidaredoxin reductase, are able to provi

54 n the electron transfer mechanism in the Pdr-putidaredoxin redox couple and their mammalian counterpa

55 huttles electrons between the NADH-dependent putidaredoxin reductase (Pdr) and cytochrome P450(cam).

56 tidaredoxin (Pdx) shuttles electrons between putidaredoxin reductase (Pdr) and P450cam and, thus, mus

57 Interaction and electron transfer between putidaredoxin reductase (Pdr) and putidaredoxin (Pdx) fr

58 ic monooxygenase that requires two proteins, putidaredoxin reductase (PdR) and putidaredoxin (Pdx), t

59 Putidaredoxin reductase (PdR) is the flavin protein that

60 pe (WT) and six-histidine tag-fused (His(6)) putidaredoxin reductase (Pdr), a FAD-containing componen

61 The crystal structure of recombinant putidaredoxin reductase (Pdr), an FAD-containing NADH-de

62 utida consists of three redox proteins: NADH-putidaredoxin reductase (Pdr), putidaredoxin (Pdx), and

63 tochrome P450cam with putidaredoxin (Pd) and putidaredoxin reductase (PdR), the two proteins required

64 ned crystal structure of a covalently linked putidaredoxin reductase (Pdr)-putidaredoxin (Pdx) comple

65 some overlap in the binding sites on Pdx for putidaredoxin reductase and CYP101.

66 process, allowing thermodynamic reduction by putidaredoxin reductase and molecular oxygen addition.

67 omonas putida, transfers electrons from NADH-putidaredoxin reductase to cytochrome P450cam.

68 t G248D) mutant with camphor, putidaredoxin, putidaredoxin reductase, and NADH results in partial cov

69 is very slowly reduced by putidaredoxin and putidaredoxin reductase, but these proteins support cata

70 as important in the interaction of Pdx with putidaredoxin reductase, whereas aspartate 38 serves a c

71 in a reaction supported by putidaredoxin and putidaredoxin reductase.

72 equivalents from bacterial putidaredoxin and putidaredoxin reductase.

73 s to [2Fe-2S] ferredoxins of the adrenodoxin/putidaredoxin subfamily of ferredoxins.

74 es binding of the heterologous redox partner putidaredoxin to CYP119 and the rate of electron transfe

75 Electron transfer from putidaredoxin to the mutant is much slower than to the w

76 t results in improved electron transfer from putidaredoxin to the P450 enzyme.

77 .14.15.1) through its natural redox partner (putidaredoxin) using an antimony-doped tin oxide working