ライフサイエンスコーパス: DCCD

1 DCCD effectively inhibited phase III of the carotenoid b

2 DCCD has two distinct effects on phase III of the electr

3 DCCD modification also inhibited the binding of 86Rb+ an

4 DCCD modification selectively inhibited the K+-dependent

5 DCCD treatment of chromatophores also slows down the kin

6 [14C]DCCD was incorporated into the H,K-ATPase in a time cour

7 parations of the H,K-ATPase modified by [14C]DCCD.

8 , SD840IM, was obtained from a 3.3-kDa, [14C]DCCD-labeled peptide resolved from a V8 digest of the pa

9 rporated into the enzyme by 1.6 nmol of [14C]DCCD/mg of protein.

10 e was K+-sensitive where K+ reduced the [14C]DCCD incorporated into the enzyme by 1.6 nmol of [14C]DC

11 A component of the [14C]DCCD incorporated into the H,K-ATPase was K+-sensitive w

12 ated tryptic peptides resolved from the [14C]DCCD-modified H,K-ATPase exhibited various K+ sensitivit

13 ed a concentration dependence with the K0.5 (DCCD) = 0.65 +/- 0.04 mM.

14 fluorescence lifetime component amplitudes, DCCD binding, and DeltaA535.

15 drolytic and H+ translocation activities and DCCD sensitivities similar to wild type.

16 ipulated by additions of HCN, nigericin, and DCCD (N,N'-dicyclohexylcarbodamide).

17 an approximately linear relationship between DCCD binding and the extent of reversal of fluorescence

18 TP synthesis and breakdown were inhibited by DCCD.

19 not E305D or D504E mutants, to inhibition by DCCD is consistent with the involvement of acidic residu

20 s the residue whose covalent modification by DCCD is responsible for the abolition of PPi-dependent H

21 gion of E. coli TatC, which when modified by DCCD interferes with the deep insertion of a Tat signal

22 ion of chlorophyll fluorescence quenching by DCCD have been investigated.

23 E. coli survival was unaffected by DCCD at any pH value tested.

24 At low concentrations, DCCD increases the magnitude of the electrogenic process

25 ation and residual activities with decreased DCCD sensitivity.

26 lants did not bind dicyclohexylcarbodiimide (DCCD), a known inhibitor of qE.

27 N,N'-dicyclohexylcarbodiimide (DCCD) has been reported to inhibit proton translocation

28 N,N'-dicyclohexylcarbodiimide (DCCD) has been reported to inhibit steady-state proton t

29 ut 100 microM N,N'-dicyclohexylcarbodiimide (DCCD), a specific inhibitor of F1F0-ATPase.

30 PPase and the N,N'-dicyclohexylcarbodiimide (DCCD)-binding transmembrane alpha-helix of the c-subunit

31 active toward N,N'-dicyclohexylcarbodiimide (DCCD).

32 the compound N,N'-dicyclohexylcarbodiimide (DCCD, DCC).

33 een the binding of dicyclohexylcarbodiimide (DCCD) to isolated light-harvesting proteins of photosyst

34 ctivating reagent, dicyclohexylcarbodiimide (DCCD).

35 llin, desfuroylceftiofur cysteine disulfide (DCCD, an antimicrobial metabolite of ceftiofur), ampicil

36 re 70% or better for all beta-lactams except DCCD, which had an average recovery of 58%.

37 specific for Fe2+ and was inhibited by FCCP, DCCD and vanadate, indicating an active process energize

38 Modification with the fluorescent DCCD analogue N-(1-pyrenyl)cyclohexylcarbodiimide, coupl

39 periments revealed only one binding site for DCCD and Na(+), indicating that the mature c subunit of

40 Cl protected 70% of the ATPase activity from DCCD-dependent inhibition in a concentration-dependent m

41 427D mutants, implicate a role for Glu427 in DCCD-insensitive H+ translocation by the V-PPase.

42 ic residues at these positions in inhibitory DCCD binding.

43 At higher concentrations (>150 microM), DCCD slows the development of phase III of the electroch

44 ontrol preparations to about 23 ms at 1.2 mM DCCD, without significantly changing the amplitude.

45 in control preparations to 8-10 ms at 0.8 mM DCCD.

46 olved in the F1 interaction became modified, DCCD inhibition was progressively lost, as was coupling

47 However, labeling with DCCD as well as Na(+)-DCCD competition experiments revealed only one binding s

48 of protein structure on both the binding of DCCD and the fluorescence quenching mechanism.

49 However, the binding of DCCD was found to occur at least an order of magnitude f

50 bc(1) complex, we investigated the effect of DCCD modification on flash-induced electron transport an

51 bc(1) complex, we investigated the effect of DCCD modification on flash-induced electron transport an

52 t specifically responsible for the effect of DCCD-induced effects of cytochrome bc(1) complex.

53 nship was obtained between the efficiency of DCCD binding and the DCCD-dependent reversal of fluoresc

54 re discussed in terms of the multiplicity of DCCD-binding sites and the influence of protein structur

55 in survival of H. pylori in the presence of DCCD compared to its absence, whereas incubation with DC

56 d type, in conjunction with the retention of DCCD inhibitability in both E427Q and E427D mutants, imp

57 To understand the possible role of DCCD in inhibiting the protonogenic reactions of cytochr

58 f the pump molecule is a significant site of DCCD modification.

59 on proton pumping-coupled ATP hydrolysis, on DCCD sensitivity of this activity, or on ATP synthesis r

60 of phase III of the electrochromic shift on DCCD concentration was identical in WT and B187DN chroma

61 diminished through slow diffusion, and only DCCD and HCN were required to elicit proton extrusion.

62 reconstituted complexes in which a putative DCCD-binding site had been mutagenized.

63 We conclude that DCCD treatment of chromatophores leads to modification o

64 Moreover, we found that DCCD mediates discrete intramolecular cross-links of E.

65 reduction of both cytochromes indicates that DCCD treatment modifies the reaction of QH(2) oxidation

66 n to cytochrome b reduction, indicating that DCCD inhibits the delivery of electrons from quinol to h

67 proton translocation, and did not alter the DCCD inhibition of ATPase activity.

68 tween the efficiency of DCCD binding and the DCCD-dependent reversal of fluorescence quenching.

69 The sensitivity of H. pylori to DCCD at pH 7 and 6, and failure to recover F1F0 H. pylor

70 r PPi hydrolysis but retained sensitivity to DCCD.

71 f carotenoids, or sensitivity of turnover to DCCD.

72 ation activity and conservation of wild type DCCD sensitivity in E229Q mutants refute the notion that

73 ared to its absence, whereas incubation with DCCD at pH 7 and 6 significantly decreased H. pylori sur

74 However, labeling with DCCD as well as Na(+)-DCCD competition experiments revea