ライフサイエンスコーパス: cytochrome P450cam

1 on substrate (camphor) binding to a protein (cytochrome P450cam).

2 n to be important for dioxygen activation by cytochrome P450cam.

3 ectrons from NADH-putidaredoxin reductase to cytochrome P450cam.

4 o 1.7 A resolution and compared with that of cytochrome P450cam.

5 ost thoroughly investigated cytochrome P450, cytochrome P450cam.

6 active site of the monooxygenase hemoprotein cytochrome P450cam.

7 in reductase (Pdr), putidaredoxin (Pdx), and cytochrome P450cam.

8 that is consistent with analogous studies of cytochrome P450cam.

9 effector in the biochemical cycle involving cytochrome P450cam.

10 matase model based on the X-ray structure of cytochrome P450cam.

11 ments with molecular dynamics simulations on cytochrome P450cam.

12 The cytochrome P450cam active site is known to be perturbed

13 from approximately 50% bacterial (cytosolic) cytochrome P450cam and 50% mammalian (membrane-bound) cy

14 ly reported for corresponding derivatives of cytochrome P450cam and document significant and importan

15 gram has been used to predict inhibitors for cytochrome P450cam and its L244A mutant.

16 roscopy is applied to the cyanide adducts of cytochrome P450cam and its T252A and D251N site-directed

17 redoxin-like Fe(2)S(2) redox partner used by cytochrome P450cam and many other bacterial P450s.

18 etween the spectra of ferric substrate-bound cytochrome P450cam and those of the exogenous ligand-fre

19 Cytochromes P450cam and P450BM3 oxidize alpha- and beta-

20 CYP101 (cytochrome P450cam) catalyses the oxidation of camphor b

21 the first electron transfer involved in the cytochrome P450cam catalytic cycle.

22 Previous crystal structures of cytochrome P450cam complexed with its redox partner, put

23 X-ray crystal structures at 1.8A and 1.5A of cytochrome P450cam complexed with two synthetic molecula

24 the effector role of Pdx (putidaredoxin) on cytochrome P450cam conformation is refined by attaching

25 bound to the active site of microcrystalline cytochrome P450cam (CP450cam) in its resting state.

26 Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket through mutage

27 Cytochrome P450cam (CYP101) from Pseudomonas putida is u

28 2Fe-2S] ferredoxin, putidaredoxin (Pdx), and cytochrome P450cam (CYP101) from the bacterium Pseudomon

29 Structural perturbations in cytochrome P450cam (CYP101) induced by the soluble fragm

30 Cytochrome P450cam (CYP101) is a prokaryotic monooxygena

31 The camphor monoxygenase cytochrome P450cam (CYP101) requires potassium ion (K+)

32 redoxin (Pdx) with its redox partners in the cytochrome P450cam (CYP101) system was investigated by s

33 of Ru-diimine complexes designed to bind to cytochrome p450cam (CYP101).

34 eved to be involved in the binding of Pdx to cytochrome P450cam (CYP101).

35 apo- (i.e., camphor-free) and camphor-bound cytochrome P450cam (CYP101).

36 A close orthologue to cytochrome P450cam (CYP101A1) that catalyzes the same hy

37 Cytochrome P450cam (CYP101Fe(3+)) regioselectively hydro

38 In the cytochrome P450cam-dependent monooxygenase system from P

39 Although cytochrome P450cam from Pseudomonas putida, the archetyp

40 g putidaredoxin (Pdx), the electron donor to cytochrome P450cam in Pseudomonas putida, was improved b

41 0cin is substantially different from that of cytochrome P450cam in that the B' helix, essential for s

42 The catalytic pathway of cytochrome P450cam is studied by means of a hybrid quant

43 hod, proton transfer into the active site of cytochrome P450cam is studied.

44 mining step in the catalytic cycle of native cytochrome P450cam is the reduction of the dioxygen comp

45 physiological role for potassium binding by cytochrome P450cam is to promote camphor binding even at

46 is nonexistent in the case of substrate-free cytochrome P450cam, is most reasonably attributed to int

47 e binding in many cytochrome P450s including cytochrome P450cam, is replaced by an ordered loop that

48 NADH-dependent flavoprotein component of the cytochrome P450cam monooxygenase from Pseudomonas putida

49 ), a FAD-containing component of the soluble cytochrome P450cam monooxygenase system from Pseudomonas

50 CO, ferric NO, and ferrous NO derivatives of cytochrome P450cam, no significant changes are observed

51 (77 K) and annealing of the ternary ferrous cytochrome P450cam-O(2)-substrate complex.

52 studies have been carried out on oxyferrous cytochrome P450cam one-electron cryoreduced by gamma-irr

53 dioxygen bound state of the D251N mutant of cytochrome P450cam (oxy-P450cam) and its complex with re

54 Cytochrome P450cam (P450cam) is the terminal monooxygena

55 cking site topography more closely resembles cytochrome P450cam than cytochrome P450BM3.

56 ry complexes of camphor, dioxygen, and ferro-cytochrome P450cam to inject the "second" electron of th

57 The redox enzyme cytochrome P450cam undergoes a multistep catalytic cycle

58 Cytochrome P450cam was subjected to high pressures of 2.

59 the ferrous dioxygen bound form of wild type cytochrome P450cam were performed and the results analyz

60 However, for the site-specific mutant D251N cytochrome P450cam (which affects proton transfer near t

61 not have the conserved threonine, Thr252 in cytochrome P450cam, which is generally considered as an

62 Reactions of substrate-free ferric cytochrome P450cam with peracids to generate Fe=O interm

63 Fusion proteins of cytochrome P450cam with putidaredoxin (Pd) and putidared