ライフサイエンスコーパス: stigmatellin

1 ive inhibitors of Q(B) binding (terbutryn or stigmatellin).

2 3-methoxy-2-(4'-trans-stilbenyl)acrylate, or stigmatellin).

3 ts signal intensity depends on the amount of stigmatellin.

4 d by the center P inhibitors myxothiazol and stigmatellin.

5 in the presence and absence of the inhibitor stigmatellin.

6 30-fold more tightly than in the absence of stigmatellin.

7 uding rotenone, fenperoximate, pyridaben, or stigmatellin.

8 axoxystrobin and pyraclostrobin, but not to stigmatellin.

9 he presence of a saturating concentration of stigmatellin.

10 e is occupied by inhibitors such as DBMIB or stigmatellin.

11 tion similar to that seen in the presence of stigmatellin.

12 could bind to its Qo site in the presence of stigmatellin.

13 a both in the presence and in the absence of stigmatellin.

14 d its interaction with the Qo site inhibitor stigmatellin.

15 ted in the Fe-S subunit confer resistance to stigmatellin.

16 d by the mitochondrial complex III inhibitor stigmatellin (20 nM) when given at reperfusion (p < .05)

17 Stigmatellin, a Q(P) site inhibitor, inhibits electron t

18 cells and treatment of wild-type cells with stigmatellin abolished reactive oxygen species (ROS) gen

19 ical formed is proportional to the amount of stigmatellin added.

20 h the quinol oxidation (Q(P)) site inhibitor stigmatellin alone or in combination with the quinone re

21 Stigmatellin, an inhibitor of the mitochondrial and phot

22 iron sulfur protein docking interface, where stigmatellin and 5-n-undecyl-6-hydroxy-4,7-dioxobenzothi

23 inhibitors azoxystrobin, MOAS, myxothiazol, stigmatellin and 5-undecyl-6-hydroxy-4,7-dioxobenzothiaz

24 Respiratory chain inhibitors stigmatellin and antimycin A, which inhibit Qo and Qi si

25 a both in the presence and in the absence of stigmatellin and had perturbed Qo site occupancy.

26 Stigmatellin and methoxyacrylate stilbene, two inhibitor

27 the bc1 complex (UQ/UQH2 and the inhibitors stigmatellin and myxothiazol) and the [2Fe-2S] cluster o

28 t that this group is involved in ligation of stigmatellin and quinol, but not quinone, and that the c

29 ondrial cyt bc(1) complex in the presence of stigmatellin and the Chlamydomonas reinhardtii cyt b(6)f

30 In addition, the levels of stigmatellin and UHDBT binding are markedly diminished,

31 uinone analog inhibitors at 3.07 A (tridecyl-stigmatellin) and 3.25-A (2-nonyl-4-hydroxyquinoline N-o

32 Reactivated complex exhibited myxothiazol, stigmatellin, and antimycin A sensitive cyt c reductase

33 hese results support the idea that UHDBT and stigmatellin arrest the [2Fe-2S] cluster at a fixed posi

34 to provide wild-type-like interactions with stigmatellin at the Qo site of the bc1 complex.

35 hereas the rate of re-reduction sensitive to stigmatellin (at Eh = 0 mV, (where Eh is the ambient red

36 Significantly, the slow stigmatellin binding phase was lost as the inhibitor con

37 center P site in the dimer to the other upon stigmatellin binding to one monomer, rendering the secon

38 posed that ISP becomes a strong oxidant upon stigmatellin binding, extracting electrons from an organ

39 us bc(1) complex, we demonstrated that while stigmatellin blocked the cleavage, myxothiazol hardly af

40 asic binding of antimycin in the presence of stigmatellin but did not slow down antimycin binding rat

41 In stigmatellin-containing crystals, the side chain points

42 From the structure of the stigmatellin-containing mitochondrial complex, we sugges

43 her by these mutations or by the addition of stigmatellin do not act synergistically.

44 L213Asp-L212Glu --> Ala-Ala (AA), the pK of stigmatellin dropped to 7.5 and 7.4, respectively, which

45 However, the inhibitor, stigmatellin, freezes the Rieske protein iron-sulfur clu

46 In contrast, stigmatellin generated an asymmetric shift in the b(L) s

47 tochrome bc1, with and without the inhibitor stigmatellin, have led to the proposal that the Rieske p

48 Measurements showed a high pK value (>11) of stigmatellin in the QB pocket of the dark-state wild-typ

49 ne mitochondrial cytochrome bc1 complex with stigmatellin in the Qo quinol binding site.

50 in the ring-in mode, as previously found for stigmatellin in X-ray structures of the cytochrome bc(1)

51 H2O2 production is blocked by stigmatellin, indicating its origin from complex III, an

52 Both myxothiazol and stigmatellin induced a 2-3 nm shift of the visible absor

53 e Q(o) pocket, the NQNO behaves similarly to stigmatellin, inducing an iron-sulfur protein conformati

54 Oxygen radicals are not generated when stigmatellin is added to a mutant bc1 complex lacking th

55 Oxygen radicals are generated when stigmatellin is added to the oxidized complex in the abs

56 organic free radical, is also observed when stigmatellin is added to the oxidized complex, and its s

57 proximately half of the center P sites bound stigmatellin more slowly and in a different position rel

58 Because the position that stigmatellin occupies at center P is considered to be an

59 er EPR spectrum, similar to those induced by stigmatellin or 2-iodo-6-isopropyl-3-methyl-2',4,4'-trin

60 an interface with cytochrome b is induced by stigmatellin or 5-n-undecyl-6-hydroxy-4,7-dioxobenzothia

61 bH heme by decylubiquinol in the presence of stigmatellin or myxothiazol were also consistent with a

62 ron transfer activity, which is sensitive to stigmatellin or myxothiazol.

63 yme when both samples were exposed to either stigmatellin or myxothiazol.

64 a of their [2Fe-2S] cluster, and response to stigmatellin or to the Qpool redox state.

65 II inhibitor myxothiazol (or MOA-stilbene or stigmatellin) or with KCN and ascorbate to reduce the hi

66 n the presence of myxothiazol, MOA-stilbene, stigmatellin, or of antimycin added to SMP pretreated wi

67 nhibitor), beta-methoxyacrylate derivatives, stigmatellin (P-side inhibitors), and ethoxyformic anhyd

68 breakdown of endogenously generated H2S with stigmatellin potentiated the amplitude of F-EPSPs evoked

69 le to sense the Qpool redox state or to bind stigmatellin properly.

70 Stigmatellin raises the midpoint potential of ISP from 2

71 Unexpectedly, they were highly resistant to stigmatellin (StiR) and hypersensitive to myxothiazol (M

72 undecyl-6-hydroxy-4, 7-dioxobenzothiazol and stigmatellin (subtype Qo-II and Qo-III, respectively) le

73 e p-side quinone-analogue inhibitor tridecyl-stigmatellin (TDS) are very similar.

74 found for the chromone ring of the tridecyl-stigmatellin (TDS) quinone analogue inhibitor, one near

75 n by atpenin A5 or complex III inhibition by stigmatellin that results in succinate-dependent reducti

76 in to the substrate quinol and the inhibitor stigmatellin, the Thermus thermophilus Rieske protein wa

77 The binding of stigmatellin to the fully oxidized complex, oxidized com

78 An even lower rate is observed with the stigmatellin-treated complex.

79 naquinol through center N in the presence of stigmatellin was approximately half of that observed whe

80 ystem of isolated RC revealed that the pK of stigmatellin was controlled overwhelmingly by electrosta

81 When stigmatellin was occupying center P, concentration-depen

82 However, in the presence of stigmatellin, we find that oxidized cytochrome c2 binds

83 ty of electron transport activity to TDS and stigmatellin were observed: (a) little effect of mutatio

84 10(5) m(-1) s(-1)) except in the presence of stigmatellin, where a second slower binding phase compri

85 ubiquinol-cytochrome c reductase activity by stigmatellin, which binds analogous to reaction intermed

86 quinol binds in a fashion similar to that of stigmatellin with H-bonds between H161 of the Rieske iro