ライフサイエンスコーパス: heme enzyme

1 roscopically observed in a histidine-ligated heme enzyme.

2 re of a thioether inhibitor complexed to any heme enzyme.

3 sm of regulation of the activity of this key heme enzyme.

4 M(IV)(O)(porph(*+)) (M = Mn or Fe) found in heme enzymes.

5 or the understanding of O-O bond cleavage in heme enzymes.

6 onding that is important for the function of heme enzymes.

7 idation of hydrocarbons by both heme and non-heme enzymes.

8 , ligand, and metal modulate the function of heme enzymes.

9 forcing drug design attempts targeting those heme enzymes.

10 AspB and reveals a new reaction manifold in heme enzymes.

11 fering opportunities for biocatalysis beyond heme enzymes.

12 for controlling reactivity across groups of heme enzymes.

13 the end-on compound 0 intermediates in other heme enzymes.

14 ained resulted in functional mimics of these heme enzymes.

15 heme-dependent aromatic oxygenases and most heme enzymes.

16 asized electric field along the Fe-O bond in heme enzymes.

17 tions that are unknown for histidine-ligated hemes enzymes.

18 Heme enzymes activate oxygen through formation of transi

19 ts add new features to SA's interaction with heme enzymes and its in vivo redox properties.

20 [Fe(IV)O] intermediate is important in many heme enzymes, and thus, the precise nature of the Fe(IV)

21 Heme enzymes are capable of catalyzing a range of oxidat

22 Heme enzymes are predominantly responsible for this conv

23 a and the properties of other well-described heme enzymes are proposed.

24 II)-O(2)*(-) intermediates are well known in heme enzymes, but none have been characterized in the no

25 MCS)+ are higher than the ones obtained with heme enzymes, but the chemoselectivity is lesser affecte

26 at fine-tuning E degrees ' in HCOs and other heme enzymes can modulate their substrate affinity, ET r

27 ins, demonstrating that non-thiolate-ligated heme enzymes can perform this function.

28 ial life processes, nature has had to evolve heme enzymes capable of synthesizing and manipulating co

29 Catalytic heme enzymes carry out a wide range of oxidations in bio

30 Catalase activity of the dual-function heme enzyme catalase-peroxidase (KatG) depends on severa

31 ommonly employed diazo compounds within iron heme enzyme-catalyzed carbene transfer reactions has bee

32 ligands and serves as a nonheme analogue for heme enzyme compounds I.

33 tuberculosis catalase-peroxidase (KatG) is a heme enzyme considered important for virulence, which is

34 We conclude that both new heme enzymes contain histidine as their proximal heme ir

35 (a) approximately 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insigh

36 In exponentially growing yeast, the heme enzyme, cytochrome c peroxidase (Ccp1) is targeted

37 orphyrin IX (Mn-PGHS) to those of the native heme enzyme (Fe-PGHS).

38 Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fu

39 The active sites of heme enzymes have evolved to control the formation of hi

40 ereoselectivity of P4H and many non-heme and heme enzymes in general, and insight into this matter ma

41 of metal-organic materials (MOMs) that mimic heme enzymes in terms of both structure and reactivity.

42 The heme enzyme indoleamine 2,3-dioxygenase (IDO) is a key r

43 The heme enzyme indoleamine 2,3-dioxygenase (IDO) plays an i

44 The heme enzyme indoleamine 2,3-dioxygenase (IDO) was found

45 The heme enzyme indoleamine 2,3-dioxygenase 1 (IDO1) plays a

46 of the axial ligand in high-valent iron-oxo heme enzyme intermediates and related synthetic catalyst

47 The heme enzyme is shown to follow the halogenation cycle th

48 yrin intermediates, inadequate activation of heme enzymes, low catalase activity, defective clearance

49 que has been used to study copper complexes, hemes, enzyme mechanisms, micellar water content, and wa

50 These heme-enzyme-mediated indole monooxygenation pathways are

51 DHP I is a heme enzyme (Mr = 30,790) composed of two identical subu

52 ithin phagosomes, superoxide reacts with the heme enzyme myeloperoxidase (MPO) and is converted to hy

53 The heme enzyme myeloperoxidase (MPO) is one of the key play

54 The heme enzyme myeloperoxidase (MPO) participates in innate

55 e oxygen species that are generated by their heme enzyme myeloperoxidase.

56 Heme enzymes provide a striking example of this complexi

57 tudies it was reported that thiolate-ligated heme enzymes react with peroxynitrite to form a ferryl i

58 Eosinophil peroxidase, a heme enzyme released by eosinophils, generates hypobromo

59 Myeloperoxidase, a heme enzyme released by polymorphonuclear neutrophils, a

60 Oxygen activation in all heme enzymes requires the formation of high oxidation st

61 erium tuberculosis KatG is a multifunctional heme enzyme responsible for activation of the antibiotic

62 Myeloperoxidase, the heme enzyme secreted by activated neutrophils and monocy

63 The pathway begins with myeloperoxidase, a heme enzyme secreted by activated neutrophils.

64 Myeloperoxidase (MPO), a heme enzyme secreted by activated phagocytes, generates

65 Myeloperoxidase, a heme enzyme secreted by activated phagocytes, uses H(2)O

66 nflammation that involves myeloperoxidase, a heme enzyme secreted by activated phagocytes.

67 ange of natural and engineered activities of heme enzymes such as cytochrome P450s, which position a

68 es and is also an essential cofactor for non-heme enzymes such as ribonucleotide reductase, the limit

69 Here, we report an engineered heme enzyme that can utilize hydroxylammonium chloride,

70 Central to this process is PrnB, a heme enzyme that catalyzes the complex transformation of

71 This presents the first example for a heme enzyme that catalyzes the enantioselective oxidatio

72 Indoleamine 2,3-dioxygenase (IDO1) is a heme enzyme that catalyzes the oxygenation of the indole

73 nganese peroxidase (MnP) is an extracellular heme enzyme that catalyzes the peroxide-dependent oxidat

74 talase is a luminal thylakoid membrane-bound heme enzyme that has not been identified previously.

75 We have engineered heme enzymes that can insert fluoroalkyl carbene interme

76 nases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrat

77 DO) and tryptophan 2,3-dioxygenase (TDO) are heme enzymes that catalyze the O(2)-dependent oxidation

78 NOS) are catalytically self-sufficient flavo-heme enzymes that generate NO from arginine (Arg) and di

79 Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide

80 and diverse superfamily of mononuclear, non-heme enzymes that perform a variety of oxidative transfo

81 Nitric oxide synthases (NOSs) are flavo-heme enzymes that require (6R)-tetrahydrobiopterin (H(4)

82 (NO), is biosynthesized by a group of flavo-heme enzymes, the nitric oxide synthases.

83 on chaperones, delivering iron to target non-heme enzymes through direct protein-protein interactions

84 tryptophan with dioxygen is mediated by two heme enzymes, tryptophan 2,3-dioxygenase (TDO) and indol

85 a plethora of metalloporphyrin complexes and heme enzymes used as electrocatalysts for small-molecule

86 The heme enzyme was shown to release hypobromous acid that m

87 Using heme enzymes, we unlock a hydrogenation pathway for the

88 Chloroperoxidase is a versatile heme enzyme which can cross over the catalytic boundarie

89 ure can be catalyzed by phenol-coupling P450 heme enzymes, which might also apply to the plant kingdo

90 Nitric-oxide synthases (NOSs) are flavo-heme enzymes whose electron transfer reactions are contr

91 atalase-peroxidases (KatGs) are bifunctional heme enzymes widely spread in archaea, bacteria, and low

92 mphitrite ornata dehaloperoxidase (DHP) is a heme enzyme with a globin structure, which is capable of

93 lations of three compound I intermediates in heme enzymes with different reactivities toward C-H bond