ライフサイエンスコーパス: apocytochrome c

1 molecule mediating contact between HCCS and apocytochrome c.

2 s heme and in complex with its cognate human apocytochrome c.

3 served as the platform for interaction with apocytochrome c.

4 cific heme-binding residues of both CcmE and apocytochrome c.

5 valent attachment of the haem to periplasmic apocytochrome c.

6 with the view that the natural substrate is apocytochrome c.

7 the iron in the haem attachment reaction to apocytochromes c.

8 sulphide bond into the haem-binding motif of apocytochromes c.

9 ion of heme with the CXXCH sequence motif in apocytochromes c.

10 asurement of the redox midpoint potential of apocytochrome c(1) indicates that neither the P nor the

11 In this study, using Rhodobacter capsulatus apocytochrome c(2) as a Ccm substrate, we demonstrate fo

12 monstrate for the first time that CcmI binds apocytochrome c(2) but not holocytochrome c(2).

13 signed to serve as a model for R. capsulatus apocytochrome c(2) have also been carried out, and an E(

14 s interaction requires a free thiol group at apocytochrome c(2) heme binding site.

15 nly the C-terminal portions of both CcmI and apocytochrome c(2) mediate this binding.

16 E(m) versus pH plots for HelX, Ccl2, and the apocytochrome c(2) model peptide were all linear over th

17 terminal domain of CcmI can also weakly bind apocytochrome c(2), but this interaction requires a free

18 ons via the conserved structural elements in apocytochrome c(2), like the heme ligating cysteines or

19 he reduction of the cysteine residues of the apocytochromes c, a prerequisite for covalent ligation t

20 can efficiently reduce the disulfide bond of apocytochrome c and also resolve a mixed disulfide bond

21 is required for the activity of CCHL toward apocytochrome c and c1 and becomes essential for the hem

22 Mitochondrial apocytochrome c and c1 are converted to their holoforms

23 hiol-independent, direct interaction between apocytochrome c and CcmG.

24 esolve a mixed disulfide bond formed between apocytochrome c and CcmH.

25 hetically made, pure Drosophila melanogaster apocytochrome c and Saccharomyces cerevisiae mitochondri

26 that the heme chaperone apoCcmE binds to the apocytochrome c and the apocytochrome c chaperone CcmI t

27 tions occurring between these components and apocytochrome c and the identity of their active Cys res

28 d Cyc2p catalyse covalent haem attachment to apocytochromes c and c(1) .

29 that Cyc2p interacts with CCHL and also with apocytochromes c and c(1) .

30 Catalysis of the thioether bonds between the apocytochromes c and heme b is mediated by the heme liga

31 ck a mitochondrial targeting sequence, e.g., apocytochrome c, and possibly Cox17, a mitochondrial cop

32 Apocytochrome c (apocyt c), which in aqueous solution is

33 chemistry of the heme attachment reaction to apocytochrome c are known in bacteria and plastids but n

34 rther show that Cys-45 of CcmH and Cys-34 of apocytochrome c are most likely to form this mixed disul

35 Using purified wild-type CcmG, CcmH, and apocytochrome c, as well as their respective Cys mutant

36 Apocytochrome c associated with yeast mitochondria in tw

37 he periplasmic reduction of the cysteines of apocytochromes c before ligation.

38 In addition we show that overexpression of apocytochrome c blocks Bax-induced apoptosis in cells.

39 Like apocytochrome c, but in contrast to holocytochrome c, Ct

40 e reduction of heme prior to its ligation to apocytochrome c by CCHL.

41 gated protein-protein interactions among the apocytochrome c, CcmG, and the heme-ligation components

42 apoCcmE binds to the apocytochrome c and the apocytochrome c chaperone CcmI to yield stable binary an

43 ubunit of the CcmFHI complex functions as an apocytochrome c chaperone during the Ccm process used by

44 nents, including CcmI, proposed to act as an apocytochrome c chaperone, R. capsulatus does not have t

45 interact with each other, forming a CcmFGHI-apocytochrome c complex.

46 In fact, all apocytochromes c containing deletions located to the car

47 th respect to heme transfer from CcmE to the apocytochromes c during heme ligation assisted by the co

48 duction of a disulphide at the CXXCH site of apocytochrome c (E(m) = -265 mV) is a thermodynamically

49 to an acceptor protein (apoCcmE for CcmC or apocytochrome c for CcmF and CcsBA) such that the heme v

50 ine, suggesting that in the absence of CccA, apocytochrome c haem binding motifs become oxidised, pre

51 removed) is substantially more ordered than apocytochrome c, having characteristics consistent with

52 sulfide bond between the Cys residues at the apocytochrome c heme-binding site (CXXCH).

53 vors the presence of a disulfide bond at the apocytochrome c heme-binding site.

54 A conserved histidine in apocytochrome c (His19 of CXXCH) supplied the second axi

55 gation to a coexpressed Bordetella pertussis apocytochrome c in an Escherichia coli mutant lacking it

56 he protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific

57 an integral role in the transfer of heme to apocytochrome c in many prokaryotes and some mitochondri

58 Mutants containing wild type apocytochrome c in mitochondria lack COX, suggesting tha

59 me c, resulting from stalling of the altered apocytochrome c in partially imported states.

60 binding, transport, and coupling of heme to apocytochrome c in the periplasm of these Gram-negative

61 e, determined by the overall conformation of apocytochrome c in the vicinity of lysine 72, appears to

62 Purified CcmG* can bind apocytochrome c in vitro, revealing for the first time a

63 ave indicated that specific heme delivery to apocytochrome c is a critical feature of the cytochrome

64 Apocytochrome c is synthesized in the cytoplasm, transpo

65 obligatory components of a minimalistic heme-apocytochrome c ligation complex in R. capsulatus.

66 tent with the stereo-specificity of the heme-apocytochrome c ligation reaction.

67 cmI interact with each other to perform heme-apocytochrome c ligation.

68 or thioreduction reactions that lead to heme-apocytochrome c ligation.

69 A site-directed mutant of apocytochrome c (lysines 5, 7, and 8 replaced by glutami

70 avourable reaction, Cyc2p does not act as an apocytochrome c or c(1) CXXCH disulphide reductase in vi

71 he Ccl2 cysteine residues are oxidized by an apocytochrome c peptide containing the CXXCH domain.

72 s27, lead to reduced mitochondrial import of apocytochrome c, resulting from stalling of the altered

73 Thus, apocytochrome c secretion is normal in each of the four

74 fide cascade that reduces a disulfide on the apocytochromes c so that two cysteine thiols are availab

75 Here we show that apocytochrome c still binds Apaf-1 and that it can block

76 ocytochrome c synthase (HCCS) binds heme and apocytochrome c substrate to catalyze this attachment, s

77 How the CcmFHI complex recognizes its apocytochrome c substrates remained unknown.

78 ut the requirements for delivery of haem and apocytochrome c substrates to produce c holocytochromes.

79 ted haem for processes besides attachment to apocytochrome c, the export of a non-haem compound throu

80 Thus, the high affinity binding of apocytochrome c to mitochondria is not directly related

81 It occurs after translocation of apocytochromes c to the p side of energy transducing mem

82 l process that occurs after translocation of apocytochromes c to the positive (p) side of energy-tran

83 Import of the altered apocytochromes c was assayed in yeast strains that overe

84 form a thioreduction pathway (HelX-->Ccl2-->apocytochrome c) whereby Ccl2 function may be highly spe

85 cient mitochondrial accumulation of forms of apocytochrome c which are incapable of having heme coval

86 eby Ccl2 function may be highly specific for apocytochromes c while HelX may act as a more general re