ライフサイエンスコーパス: cytochrome bc1 complex

1 ite and fungal respiration by binding to the cytochrome bc1 complex.

2 tivity toward ilicicolin H originated in the cytochrome bc1 complex.

3 are very similar to those in the respiratory cytochrome bc1 complex.

4 , binds to the quinone reduction site of the cytochrome bc1 complex.

5 ound ubihydroquinone to cytochrome c1 of the cytochrome bc1 complex.

6 hat it may exert a cost on efficiency of the cytochrome bc1 complex.

7 ing ubiquinol oxidation by the mitochondrial cytochrome bc1 complex.

8 l from the RC, for eventual reduction of the cytochrome bc1 complex.

9 rbing the electron transfer reactions of the cytochrome bc1 complex.

10 to act on these organisms by inhibiting the cytochrome bc1 complex.

11 me b6c1 complex were similar to those of the cytochrome bc1 complex.

12 in the Qi or Qo sites, respectively, of the cytochrome bc1 complex.

13 ved in the assembly of this protein into the cytochrome bc1 complex.

14 creases the activation energy barrier of the cytochrome bc1 complex.

15 nerated during electron transfer through the cytochrome bc1 complex.

16 e for subunit 6 (Qcr6p) of the mitochondrial cytochrome bc1 complex.

17 energy of the reactions of cytochrome c with cytochrome bc1 complex.

18 d for the isolation of His-tagged complement cytochrome bc1 complex, a two-subunit complex (cytochrom

19 r the isolation of the His-tagged complement cytochrome bc1 complex, a two-subunit complex (cytochrom

20 of antimycobacterial compounds inhibits the cytochrome bc1 complex, a validated drug target in M. tu

21 The cytochrome bc1 complex activities of these membranes and

22 PSA-CSC mutant ICM contains 20 or 0% of the cytochrome bc1 complex activity found in the complement

23 -PLP mutant membranes have 10 and 30% of the cytochrome bc1 complex activity found in the complement

24 The loss of cytochrome bc1 complex activity in the ALA-PLP and ADV-P

25 The loss of cytochrome bc1 complex activity in the DeltaADV membrane

26 brane (ICM) prepared from these mutants have cytochrome bc1 complex activity similar to that in the c

27 reas the ADV-PPP mutant membrane contains no cytochrome bc1 complex activity.

28 drial electron transport at the level of the cytochrome bc1 complex and collapses mitochondrial membr

29 transport through the parasite mitochondrial cytochrome bc1 complex and collapses the mitochondrial m

30 wo-electron oxidation of quinol (QH2) at the cytochrome bc1 complex and related complexes impose dist

31 The structure determinations of the cytochrome bc1 complex and the prokaryotic potassium cha

32 ved between the bacterial (or mitochondrial) cytochrome bc1 complexes and the chloroplast cytochrome

33 inhibitors which act at defined sites in the cytochrome bc1 complex, and the optical properties of cy

34 c changes the rate of electron transfer with cytochrome bc1 complex as would be predicted by Marcus'

35 Q(H2)-loop mechanism (similar to that of the cytochrome bc1 complex) as originally proposed by Musser

36 plex is similar to the analogous respiratory cytochrome bc1 complex, but the domain arrangement outsi

37 ectrons through the respiratory chain at the cytochrome bc1 complex, causing a leak of reducing equiv

38 ned after identifying quinol turnover at the cytochrome bc1 complex (cytbc1) as rate limiting and ass

39 luding inhibition of the QcrB subunit of the cytochrome bc1 complex, disruption of cell-wall homeosta

40 tus cytochrome c2 and its K93P mutant to the cytochrome bc1 complex embedded in a phospholipid bilaye

41 Although the spectra of cytochrome bc1 complex from Rh. capsulatus are of somewh

42 ave modified the cytochrome b subunit of the cytochrome bc1 complex from the purple bacterium Rhodoba

43 Sequence alignment of cytochrome b of the cytochrome bc1 complex from various sources reveals that

44 iobacterial complex are compared to those of cytochrome bc1 complexes from purple bacteria and of cyt

45 oquinone-cytochrome c oxidoreductase (or the cytochrome bc1 complex) from Rhodobacter capsulatus is c

46 ve phosphorylation system, in particular the cytochrome bc1 (complex III)-cytochrome c oxidase (compl

47 mbled into a functionally active form in the cytochrome bc1 complex in S. cerevisiae.

48 Structure analysis of the cytochrome bc1 complex in the presence and absence of Qp

49 ecause addition of MCLA to antimycin-treated cytochrome bc1 complex, in the presence of catalytic amo

50 it was highly sensitive to inhibitors of the cytochrome bc1 complex, including antimycin A, and the r

51 Crystal structures of the cytochrome bc1 complex indicate that the catalytic domai

52 at the lack of MPP activity in the mammalian cytochrome bc1 complex is because of binding of an inhib

53 The iron-sulfur protein of the cytochrome bc1 complex is one of a small number of prote

54 The iron-sulfur proteins of the cytochrome bc1 complexes of Schizosaccharomyces pombe an

55 Mitochondrial cytochrome bc1 complex performs two functions: It is a r

56 l 4-(1H)-quinolone scaffolds that target the cytochrome bc1 complex Qi site, of which, a substituted

57 The cytochrome bc1 complex recycles one of the two electrons

58 The cytochrome bc1 complex resides in the inner membrane of

59 O-2 during the oxidation of ubiquinol by the cytochrome bc1 complex results from a leakage of the sec

60 y solved crystal structure of the vertebrate cytochrome bc1 complex revealed a discrete cavity in whi

61 study the role of this fragment in bacterial cytochrome bc1 complex, Rhodobacter sphaeroides mutants

62 ism of bifurcated oxidation of quinol in the cytochrome bc1 complex, Rhodobacter sphaeroides mutants,

63 ld reduction in the in vitro activity of the cytochrome bc1 complex, suggesting that it may exert a c

64 ctural analysis of the dimeric mitochondrial cytochrome bc1 complex suggests that electron transfer b

65 e-dimensional structure of the mitochondrial cytochrome bc1 complex suggests that movement of the ext

66 The crystal structure of the mitochondrial cytochrome bc1 complex suggests that movement of the ext

67 s expression of cytochromes c2, c(y) and the cytochrome bc1 complex that are involved in both photosy

68 ily observed with a sample of Rh. capsulatus cytochrome bc1 complex that had been uniformly labeled w

69 together with the unmodified subunits of the cytochrome bc1 complex, they formed a novel enzyme, name

70 ytochrome b increased the sensitivity of the cytochrome bc1 complex to atovaquone.

71 Antimycin A, a specific inhibitor of the cytochrome bc1 complex (ubiquinol:cytochrome c oxidoredu

72 rotein in a sample of Rhodobacter capsulatus cytochrome bc1 complex uniformly labeled with 15N but no

73 Activity of the cytochrome bc1 complex was decreased 50, 90, 67, 89, and

74 Only cytochrome c1 of the cytochrome bc1 complex was present in FJM13 cells grown

75 siae and its assembly into the mitochondrial cytochrome bc1 complex we used iron-sulfur proteins in w

76 assembly of the iron-sulfur protein into the cytochrome bc1 complex, we mutagenized the presequence o

77 els of most protein components of the bovine cytochrome bc1 complex were built, including core 1, cor

78 Notably, QcrA is a component of the cytochrome bc1 complex, which is conserved from bacteria

79 ed in crystalline bovine heart mitochondrial cytochrome bc1 complex, which possesses full electron tr

80 cytochrome c1 of the Rhodobacter sphaeroides cytochrome bc1 complex with Lys and Leu lowers the redox

81 a single crystal of the bovine mitochondrial cytochrome bc1 complex with stigmatellin in the Qo quino

82 Cocrystallization of the cytochrome bc1 complex with the 4(1H)-pyridone class of

83 er sphaeroides mutants expressing His-tagged cytochrome bc1 complexes with altered ISP necks (residue

84 er sphaeroides mutants expressing His-tagged cytochrome bc1 complexes with cysteine substitution at v

85 We have analyzed crystal structures of cytochrome bc1 complexes with electron transfer inhibito

86 er sphaeroides mutants expressing His-tagged cytochrome bc1 complexes with progressive deletion from