ライフサイエンスコーパス: flavin semiquinone

1 n both forms of the enzyme, the radical is a flavin semiquinone.

2 d with the oxidation of FMN to give a stable flavin semiquinone.

3 R spectroscopy confirms the formation of the flavin semiquinone.

4 spectra suggested the presence of a neutral flavin semiquinone.

5 ormation of the triplet diradical complex of flavin semiquinone and (*)OOH.

6 MTOX forms an anionic flavin semiquinone and a reversible, covalent flavin-sul

7 The lack of dissociation of the flavin semiquinone and chorismate from the enzyme appear

8 tribute to the relative stabilization of the flavin semiquinone and may be at least partially respons

9 sites was reduced to its respective anionic flavin semiquinone and used for measuring inter-flavin d

10 a spectral intermediate characteristic of a flavin semiquinone, and all reduced enzyme species could

11 on reduced active P450BM3 is formed with two flavin semiquinones, anionic and neutral, present simult

12 eduction state does not exceed two, with two flavin semiquinones, anionic and neutral, present.

13 duct, but only small amounts of intermediate flavin semiquinone are observed during reductive titrati

14 hydroquinone as a single electron reductant, flavin semiquinone as the hydrogen atom source, and the

15 vin in PyrDb, by iron-sulfur centers through flavin semiquinones as intermediates.

16 e that the presence of a short-lived anionic flavin semiquinone (ASQ) is not sufficient to infer the

17 the formed protonated superoxide and anionic flavin semiquinone at N5, before elimination of water af

18 or betaine aldehyde were consistent with the flavin semiquinone being not involved in catalysis.

19 increase the thermodynamic stability of the flavin semiquinone by 10-fold relative to the semiquinon

20 irectly affects the stability of the neutral flavin semiquinone by facilitating a strong and critical

21 ) CM(-)(1)) due to the presence of a neutral flavin semiquinone, can then be quantitatively reconstru

22 Measurements of the flavin semiquinone content, rate constant for NADPH rele

23 ogen-bonding interaction that stabilizes the flavin semiquinone, contributing to the low potential of

24 strate-dependent accumulation of the neutral flavin semiquinone during both the flavoenzyme reduction

25 evidence for the presence of a neutral, blue flavin semiquinone during the reduction.

26 dithionite-dependent transient formation of flavin semiquinone during turnover of (6S)-6-fluoro-EPSP

27 as coupling to the two 2Fe-2S centers or the flavin semiquinone evident.

28 e dark state and photoreduced to the neutral flavin semiquinone (FADH degrees ) in its lit state.

29 d in the oxidized enzyme, whereas an anionic flavin-semiquinone has been reported in the reduced enzy

30 l hydroquinone, with no stabilization of the flavin semiquinone; in contrast, the anionic semiquinone

31 Blue, neutral flavin semiquinone is also generated in high yields duri

32 characterization of both anionic and neutral flavin semiquinone is presented.

33 First, electrons from the ETF flavin semiquinone may enter the ETF-QO flavin one by on

34 dithionite first produces some neutral, blue flavin semiquinone radical and, finally, fully reduced F

35 We have characterized the nNOS heme iron and flavin semiquinone radical by electron paramagnetic reso

36 y different relaxation behavior and a stable flavin semiquinone radical identified by EPR as a neutra

37 protein as isolated contained an air-stable flavin semiquinone radical that was sensitive to FeCN6 o

38 A stable neutral flavin-semiquinone radical is observed in the air-oxidiz

39 A neutral flavin-semiquinone radical is observed in the oxidized e

40 ite-reduced enzyme exhibits a stable anionic flavin-semiquinone radical.

41 ed reductase domain with NADPH indicated the flavin semiquinone re-formed after addition of 1-electro

42 constant of at least 72,000 M-1 s-1, whereas flavin semiquinone reduces oxygen to form superoxide as

43 In each case, blue neutral flavin semiquinone species are stabilized on both flavin

44 along with the stabilization of the neutral flavin semiquinone, suggests the presence of a weak posi

45 destabilization of the one-electron-reduced flavin semiquinone that is differentially expressed in t

46 he formation of the blue neutral form of the flavin semiquinone, that of the semiquinone-hydroquinone

47 he catalytic cycle is electron transfer from flavin semiquinone to b2-heme.

48 ave been devised to convert the enzyme-bound flavin semiquinone to oxidized FAD and vice versa, allow

49 fficult to achieve complete reduction of the flavin semiquinone to the hydroquinone.

50 No flavin semiquinone was observed during potentiometric ti

51 The enzyme-bound anionic flavin semiquinone was unusually insensitive to oxygen o

52 l may arise from a single, extremely stable, flavin semiquinone, which becomes deprotonated upon redu

53 % thermodynamic stabilization of the anionic flavin semiquinone, while no detectable amount of semiqu

54 elevant reduced form of enzyme is an anionic flavin semiquinone, whose formation requires the substra

55 The neutral form of the flavin semiquinone, with maxima at 536 and 342 nm, is ki