ライフサイエンスコーパス: dismutation

1 n, 2 common target genes involved in radical dismutation.

2 -aerobic respiration and fermentative malate dismutation.

3 for the electrostatic facilitation of O(2)() dismutation.

4 atic contribution to the catalysis of O(2)() dismutation.

5 to O(-.2), which generated H(2)O(2) through dismutation.

6 bition of Y34F during the catalysis of O-(2) dismutation.

7 hemoglobin autoxidation because of its rapid dismutation.

8 g-lived mutants in C. elegans utilize malate dismutation, a byproduct of which is the generation of f

9 activity of MbFeIII, thus facilitating H2O2 dismutation accompanied by O2 evolution and providing pr

10 ne copper ion per subunit and have identical dismutation activities.

11 This small residual H2O2-dismutation activity is attributed to adventitious metal

12 free radical-generating activity, while its dismutation activity is identical to that of the wild-ty

13 sidue is detrimental to the chlorination and dismutation activity of chloroperoxidase.

14 are not associated with the reduction in the dismutation activity of the mutant enzyme.

15 Although the H2O2-dismutation activity was completely eliminated by these

16 le exhibited only 0.02% of the original H2O2-dismutation activity when assayed in the presence of 20

17 -free PSII membranes did not induce any H2O2-dismutation activity.

18 ne copper ion per subunit and have identical dismutation activity.

19 during proteolysis and must be detoxified by dismutation and polymerization, respectively.

20 factors influence energy metabolism, radical dismutation, and expression of survival proteins.

21 The O2*- was converted to H2O2 by dismutation, and the H2O2 was detoxified by accelerated

22 necessary for maximal activity in superoxide dismutation, appears to have no role in stabilization an

23 maximal velocity of catalysis of superoxide dismutation as compared with wild type.

24 esults with respect to the mechanism of O2*- dismutation by MnSOD are discussed.

25 pothesized this was enabled through chlorite dismutation by the community, as most strains in the Bar

26 ase in the catalysis by Mn-SOD of superoxide dismutation can be reached through both the forward (O-(

27 d rates of intracellular O2- production, O2- dismutation, dehydratase inactivation, and enzyme repair

28 At high [O(2)(-)], the dismutation efficiencies of the yeast MnSODs surpass tho

29 ratios of enzyme to superoxide radical, the dismutation efficiencies scaled as Drad MnSOD > E. coli

30 erified the beneficial effects of superoxide dismutation in cells, we then evaluated the effects usin

31 superoxide kills cells entirely through its dismutation into H(2)O(2).

32 duction in the hydrophobic heme pocket where dismutation is slow.

33 mal hydrogen electrode, whereas the rates of dismutation (kcat) are 6.0 x 10(7), 4.1 x 10(6), and 3.8

34 e chloride channel(s) and that SOD1-mediated dismutation of *O(2)(-) at the endosomal surface may pro

35 The slow phase is dismutation of a pair of molecules of two-electron reduc

36 etry results, Cld is highly specific for the dismutation of chlorite to chloride and dioxygen with no

37 homogeneous electron distribution due to the dismutation of formal oxidation numbers as compared with

38 During dismutation of H2O2, [TPL] and [MbFeIV] remained constan

39 yme superoxide dismutase (SOD) catalyzes the dismutation of highly reactive O2 (-) into H2O2 and thus

40 oxidase-specific substrate, and catalase for dismutation of hydrogen peroxide generated in the enzyme

41 r manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting betwee

42 Dismutation of mROS by manganese superoxide dismutase ov

43 H(2)O(2) was generated in part by dismutation of O(2)(.) and served as a precursor for OH.

44 he formation of .OH adducts from spontaneous dismutation of O-2 and concomitant reaction with H2O2.

45 ensity of the .OH adduct by accelerating the dismutation of O-2.

46 H2O2 in bolus or generated from the dismutation of O2- by SOD, was cytotoxic at high concent

47 l of cellular superoxide anion (O2-.) is the dismutation of O2-. to hydrogen peroxide by the enzyme s

48 ndrial function (attenuated capacity for the dismutation of reactive oxygen species) and diminished i

49 is the antioxidant enzyme that catalyzes the dismutation of superoxide (O2*-) to O2 and H2O2.

50 the enhancing capacity of Cu/Zn-SOD, and the dismutation of superoxide anion radicals generated from

51 ine of antioxidant defense by catalyzing the dismutation of superoxide anion radicals to form hydroge

52 se A (sodA, bb0153), an enzyme mediating the dismutation of superoxide anions and examined the in vit

53 their enzymic activities for catalyzing the dismutation of superoxide anions and the generation of f

54 SOD, which catalyses the dismutation of superoxide into hydrogen peroxide, should

55 anion accelerates this reaction because the dismutation of superoxide leads to increased levels of h

56 t to the accepted mechanism of SOD catalysed dismutation of superoxide operates, with Cu(I) oxidation

57 Superoxide dismutases (SODs) catalyze the dismutation of superoxide radicals in a broad range of o

58 Its primary function is catalysing the dismutation of superoxide to O(2) and H(2)O(2).

59 , an enzyme that induces the rapid catalytic dismutation of superoxide to the less reactive H(2)O(2)

60 entadecane (MnBAM) effectively catalyzed the dismutation of superoxide with catalytic rate constants

61 which were caused by proton consumption upon dismutation of superoxide, followed by activation of a v

62 oxide radical and the H2O2 produced from the dismutation of superoxide, respectively, and thus preven

63 In a concerted effort, SOD will catalyze the dismutation of superoxide, resulting in the elimination

64 nd Fe(II) ions are capable of catalyzing the dismutation of superoxide, solutions of Ni(II) are not.

65 determined rate constants for the catalytic dismutation of superoxide.

66 Dehydroascorbic acid is generated by dismutation of the ascorbyl free radical, and thioredoxi

67 and showed a hydride transfer which led to a dismutation of the intermediate species.

68 ion markTrx-SOD is capable of catalyzing the dismutation of the superoxide anion; comparative studies

69 xide dismutase ( SOD1 ), which catalyses the dismutation of the superoxide radical to hydrogen peroxi

70 eroxide dismutase (SOD), which catalyzes the dismutation of the superoxide radical, is present in the

71 O2*) trapping by CPCOMPO and the spontaneous dismutation of this radical in aqueous media.

72 ric metal-binding enzyme responsible for the dismutation of toxic superoxide to hydrogen peroxide and

73 ADPH oxidase-derived superoxide, but not its dismutation product H2O2.

74 nt formation of superoxide (O2 (.-)) and its dismutation product hydrogen peroxide (H2O2) as determin

75 inverted question markTrx-SOD catalyzes the dismutation reaction at a rate on the order of 10(5) M-1

76 dentified as a major source of the dark H2O2-dismutation reaction in PSII membrane samples.

77 In the presence of excess NADH, this dismutation reaction is followed by the rapid reaction o

78 e fast component appears to correlate with a dismutation reaction occurring with the flavin.

79 the structural changes that occur during the dismutation reaction of hydrochlorofluorocarbon-22 (CHCl

80 sequent kinetic measurements reveal that the dismutation reaction proceeds in two discrete steps and

81 proposed to generate singlet oxygen through dismutation reaction, resulting in a low yield of (1)O(2

82 s subsequently undergo an enzyme-independent dismutation reaction, the rate of which is decreased whe

83 6-13) than be accounted for by simple O2(-) dismutation (RH/RH2O2 = 2), implying a significant oxida

84 (2), produced as a consequence of superoxide dismutation, stimulates vascular cell proliferation and

85 alternate energy production pathway, malate dismutation, that is operative in these animals.

86 , mitochondrial anion channels and cytosolic dismutation to H2O2 may be important steps for oxidant i

87 eroxide, either directly or through its self-dismutation to H2O2, is likewise believed to be a cell-s

88 ese and in efficient catalysis of superoxide dismutation to oxygen and hydrogen peroxide.

89 (-1), suggesting that cvSOD-catalyzed O2 (-) dismutation was not a diffusion controlled encounter.