ライフサイエンスコーパス: copper oxidase

1 ream of yacK, which encodes a putative multi-copper oxidase.

2 ting as electron entry port in terminal heme-copper oxidases.

3 for redox-regulated proton transfer in heme-copper oxidases.

4 ily of enzymes that includes all of the heme-copper oxidases.

5 absolutely conserved in all other known heme-copper oxidases.

6 s (YH) moiety at the active site of the heme-copper oxidases.

7 diverged members of the superfamily of heme/copper oxidases.

8 C(epsilon) Tyr) biring structure in the heme-copper oxidases.

9 ng) is critical for the function of the heme copper oxidases.

10 types of Cu(II) sites found in multinuclear copper oxidases.

11 ext of the proton pump mechanism of the heme-copper oxidases.

12 eavage and proton-pumping mechanisms of heme-copper oxidases.

13 phodiesterases (6), phytocyanins (25), multi-copper oxidases (2), extensins (6), plasma membrane rece

14 The crystal structure of blue copper oxidase, a type C two-domain multicopper oxidase

15 hydroxyl group of heme o in modulating heme-copper oxidase activity through participation in an extr

16 the product of this gene may function like a copper oxidase and that it may be directly responsible f

17 chrome c oxidase (CcO), a mitochondrial heme-copper oxidase and the terminal enzyme of the mitochondr

18 oxide at the bimetallic active sites of heme-copper oxidases and nitric oxide reductases.

19 e later stages of dioxygen reduction in heme-copper oxidases and show that E286 is an important compo

20 t NOR is indeed structurally related to heme-copper oxidases and that it contains a heme/non-heme iro

21 rved copper binding motifs characteristic of copper oxidases, and no enzymatic function could be assi

22 out of the specialized channels of the heme-copper oxidases are generally not well understood.

23 s of the bimetallic active sites in the heme-copper oxidases are reviewed.

24 ochondria and many aerobic prokaryotes, heme-copper oxidases are the terminal enzymes that couple the

25 Heme-copper oxidases are transmembrane enzymes involved in ae

26 that is related structurally to the multiple-copper oxidases ascorbate oxidase and laccase.

27 te that cytochrome bd oxidases like the heme-copper oxidases break the O-O bond in a single four-elec

28 The heme-copper oxidases convert the free energy liberated in the

29 mental iron uptake system orthologous to the copper oxidase-dependent Fe(III) uptake system of Saccha

30 is a member of the family of radical-coupled copper oxidases, enzymes containing a free radical coord

31 showed significant similarity to other blue copper oxidases, especially with respect to the copper-b

32 The Fet3 protein (Fet3p) is a multinuclear copper oxidase essential for high-affinity iron uptake i

33 thermus thermophilus, a homolog of the heme-copper oxidase family, have been cloned.

34 ligand-binding activity typical of the heme-copper oxidase family.

35 eavage of the oxygen-oxygen bond by the heme-copper oxidases forms the key intermediate P(M), which i

36 ping mechanism presumably common to all heme-copper oxidases has been established.

37 Haem-copper oxidase (HCO) catalyses the natural reduction of

38 s the mechanism of O-O bond cleavage in heme-copper oxidase (HCO) enzymes, combining experimental and

39 Heme-copper oxidase (HCO) is a class of respiratory enzymes t

40 metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzy

41 Cytochrome c oxidase (CcO) is a heme copper oxidase (HCO) that catalyzes the natural reductio

42 probe the role of copper and protons in heme-copper oxidase (HCO), we have performed kinetic studies

43 b, a structural and functional model of heme-copper oxidase (HCO).

44 Heme-copper oxidases (HCO), nitric oxide reductases (NOR), an

45 mino acid that plays important roles in heme-copper oxidases (HCO).

46 Heme-copper oxidases (HCOs) are key enzymes in prokaryotes an

47 Heme-copper oxidases (HCOs) catalyze efficient reduction of o

48 alogous to the chemistry carried out in heme-copper oxidases (HCOs).

49 of Fe2+ to Fe3+, by identification of yeast copper oxidases homologous to Cp that facilitate high af

50 s showing an essential role for a homologous copper oxidase in iron metabolism in yeast.

51 to produce a stable peroxide intermediate in copper oxidases in which the full complement of copper a

52 ith crystallographic structural data of heme-copper oxidases, indicate that R481 plays a keystone rol

53 Blue copper oxidase is a trimer, of which each subunit compri

54 ells, and reoxidation to ferric (FeIII) by a copper oxidase is part of the transport process.

55 Although the overall architecture of blue copper oxidase is similar to nitrite reductases, detaile

56 nd dynamics of the ligand channel(s) in heme-copper oxidases is critical for understanding how the pr

57 Laccases are a class of multi-copper oxidases (MCOs) that catalyze the one-electron ox

58 the redox-linked enzymatic reactions of heme-copper oxidases, probably because of their different bin

59 nces of the homologous subunit in other heme-copper oxidases shows that this residue is virtually tot

60 This enzyme is a member of the heme-copper oxidase superfamily and is thus crucial for dioxy

61 quinol oxidases that are members of the heme-copper oxidase superfamily have a homologous subunit II,

62 cNORs are members of the heme-copper oxidase superfamily of integral membrane proteins

63 hrome cbb3 oxidases are members of the haeme-copper oxidase superfamily that are important for energy

64 e c oxidase (cbb(3)-Cox) belongs to the heme-copper oxidase superfamily, and its subunits are encoded

65 e considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and

66 ermophilus, two distinct members of the heme-copper oxidase superfamily, were immobilized on electrod

67 from E. coli is highly conserved in the heme-copper oxidase superfamily.

68 fungal enzyme galactose oxidase is a radical copper oxidase that catalyzes the oxidation of a broad r

69 longs to the superfamily of respiratory heme-copper oxidases that couple the reduction of molecular o

70 ed this protein in the class of multinuclear copper oxidases that includes ceruloplasmin.

71 tion is the primary goal of research on heme-copper oxidases the terminal complex in the membrane-bou

72 protons have been characterized in the heme-copper oxidases: the D-channel and the K-channel.

73 In the other heme-copper oxidases, this tyrosine is known to be subject to

74 An example is given for the blue copper oxidase, Trametes versicolor laccase, in which th

75 ndings strongly suggest that all of the heme-copper oxidases utilize the same catalytic mechanism and

76 ization of novel Escherichia coli CueO multi-copper oxidase variants engineered to recapitulate prote

77 secondary hydroxyl group of heme a/o in heme-copper oxidases, we incorporated Fe(III)-2,4 (4,2) hydro

78 herichia coli is one of the respiratory heme-copper oxidases which catalyze the reduction of O2 to wa