ライフサイエンスコーパス: MnP

1 MnP also oxidized the alpha-keto dimeric product (IV) to

2 MnP is unique among Mn binding enzymes in its ability to

3 MnP provides a compelling and potentially generalizable

4 MnPs increased steady-state concentrations of Asc*- upon

5 MnPs with distinct and tunable pharmacokinetic propertie

6 is(phosphonic acid)-2,2'-bipyridine)(CO)3 ] (MnP), immobilized on a mesoporous TiO2 electrode.

7 Sm(III) was removed from a MnP-Sm(III) crystal by soaking the crystal in oxalate an

8 ectronic and magnetic properties of adsorbed MnP and approximately 0.1 A changes in the Mn-nitrogen d

9 tial up-regulation of several desaturase and MnP genes in wood-containing medium.

10 k(cat) values for ferrocyanide oxidation by MnP were not affected by the F190Y, F190L, or F190I muta

11 ting efficient MnII binding and oxidation by MnP.

12 alpha position and subsequently oxidized by MnP in the presence of Tween 80, yields of 3,4-diethoxyb

13 peroxidase (LiP), oxidation of substrates by MnP did not proceed under anaerobic conditions.

14 ns that had minimal effects alone, combining MnPs and AscH- synergized to decrease clonogenic surviva

15 to the unconventional properties of created MnP magnetic clusters within the host material.

16 Three different MnPs were tested (MnTBAP, MnT2EPyP, and MnT4MPyP), exhib

17 ible spectra of both the wild-type and F190I MnP exhibit absorption maxima at 429, 529, and 558 nm, r

18 Finally, MnP oxidized the substrate 1-(3',5'-dimethoxyphenyl)-1-h

19 (EF) are found to increase with pressure for MnP, which lead to the increase of TC of MnP.

20 s the first reports of partial sequences for MnPs in the Hymenochaetales and Corticiales.

21 c order in the itinerant-electron helimagnet MnP via the application of high pressure makes MnP the f

22 MS identified MnP proteins in C. subvermispora culture filtrates, but

23 similar Mn(II)-binding affinity and improved MnP activity, but also weakened the Fe(III)-N(His) bond

24 te, 18 s-1), but also significantly improved MnP activity in MnCcP (MnCcP(W51F, W191F): specific acti

25 In MnP and other fungal peroxidases, the Trp is replaced by

26 se results demonstrate that D242 and F190 in MnP influence the electronic environment around the heme

27 technique, we reveal a spiral spin order in MnP and trace its pressure evolution towards superconduc

28 of a tryptophan residue at this position in MnP is the main reason for the formation of an intermedi

29 n particular, mutation of the E39 residue in MnP decreases both Mn binding and oxidation.

30 there is only one major MnII binding site in MnP.

31 e MnCcP(W51F) showed significantly increased MnP activity relative to MnCcP (specific activity, 3.2 m

32 ous reduction of the oxidized intermediates, MnP compounds I and II, were dramatically increased for

33 crylamide/pectin, 94%, 98%, 88% for laccase, MnP and LiP encapsulated respectively into polyacrylamid

34 respectively; to 94%, 97%, 93% for laccase, MnP and LiP entrapped into Polyacrylamide/pectin, 94%, 9

35 / gelatine and to 87%, 91%, 87% for laccase, MnP and LiP entrapped, respectively into polyacrylamide/

36 P via the application of high pressure makes MnP the first Mn-based superconductor.

37 pothesized that catalytic manganoporphyrins (MnP) would increase AscH- oxidation rates, thereby incre

38 ing the next generation of MnCcP that mimics MnP more closely.

39 r ferrocyanide oxidation by the F190A mutant MnP was approximately 1/8 of that for the wild-type enzy

40 ximately 2 pH units lower in an F190I mutant MnP when compared to the wild-type enzyme.

41 ated that the heme environment of the mutant MnP proteins also was similar to that of the wild-type p

42 kinetic analyses of the E35Q and E39Q mutant MnPs yielded K(m) values for the substrate MnII that wer

43 properties of the wild-type and F190 mutant MnPs were examined as a function of pH.

44 or compound I (MnPI) reduction of the mutant MnPs by Mn(II) were approximately 10-fold lower than for

45 hat the similar features displayed by native MnP are largely intrinsic to the manganese oxidation rea

46 complementary strategies for developing new MnPs as Gd-free CAs with optimized biocompatibility were

47 role in stabilizing the heme environment of MnP.

48 42 is hydrogen bonded to the proximal His of MnP; in other peroxidases, this conserved Asp, in turn,

49 These results support the importance of MnP and a lignin degradation mechanism whereby cleavage

50 ues calculated from the first-order plots of MnP compound II (MnPII) reduction by Mn(II) for the muta

51 ulations, where the structural properties of MnP indicate magnetic transitions as function of pressur

52 irst-order rate constant for the reaction of MnP compound II with chelated Mn(2+) from 233 s(-1) (wil

53 t-state kinetic analysis of the reduction of MnP compound II by MnII allowed the determination of the

54 ingle disulfide bond in the distal region of MnP resulted in an enzyme that maintained a pentacoordin

55 This is also the first report of MnP-inhibitor complex structures.

56 The proposed MnII binding site of MnP consists of a heme propionate, three acidic ligands

57 the Mn ligands within the Mn binding site of MnP is essential for the efficient binding, oxidation, a

58 es of both the native and oxidized states of MnP were significantly affected by several of the mutati

59 The new 1.45 A crystal structure of MnP complexed with Mn(II) provides a more accurate view

60 d superconducting critical temperature TC of MnP sharply increases near the critical pressure PC appr

61 for MnP, which lead to the increase of TC of MnP.

62 and the E35D--E39D--D179E triple variant of MnP isozyme 1 from Phanerochaete chrysosporium.

63 multistep pathway is initiated by a LiP- or MnP-catalyzed oxidative dechlorination reaction to produ

64 rochaete chrysosporium manganese peroxidase (MnP) [isoenzyme H4] was engineered with additional disul

65 Trp51 and Trp191 while manganese peroxidase (MnP) contains phenylalanine residues at the correspondin

66 Purified manganese peroxidase (MnP) from Phanerochaete chrysosporium oxidizes nonphenol

67 Manganese peroxidase (MnP) from Phanerochaete chrysosporium undergoes a pH-dep

68 se that closely mimics manganese peroxidase (MnP) has been characterized by both one- and two-dimensi

69 Manganese peroxidase (MnP) is a heme-containing enzyme produced by white-rot f

70 Manganese peroxidase (MnP) is an extracellular heme enzyme that catalyzes the

71 ally active models for manganese peroxidase (MnP) is described.

72 Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degra

73 gnin degrading enzymes manganese peroxidase (MnP), lignin peroxidase (LiP), and versatile peroxidase

74 7.9% for free laccase, manganese peroxidase (MnP), lignin peroxidase (LiP), respectively; to 94%, 97%

75 comparable to that of manganese peroxidase (MnP).

76 n peroxidase (LiP) and manganese peroxidase (MnP).

77 mutagenesis was performed on Mn peroxidase (MnP) from the white-rot fungus Phanerochaete chrysospori

78 The mutant manganese peroxidases (MnPs) were purified and characterized.

79 geometry of the isolated manganese porphine (MnP) molecule.

80 Mn(III) porphyrin (MnP) holds the promise of addressing the emerging challe

81 gth is similar to that of the target protein MnP.

82 tely 20-fold greater for the R177A and R177K MnPs than for wild-type MnP.

83 riven CO2 reduction with the light-sensitive MnP catalyst.

84 that the TC of MnAs and MnSb are higher than MnP, implying that the MnAs and MnSb may be the more pot

85 We concluded that MnPs increase the rate of oxidation of AscH- to leverage

86 cat) value for ferrocyanide oxidation by the MnP F190A mutant was approximately 4-fold greater than t

87 hese results, we propose a mechanism for the MnP-catalyzed oxidation of these dimers, involving hydro

88 oss the 3d transition metal compounds in the MnP family, the magnetic ground state switches between a

89 contributes significantly to increasing the MnP activity because this mutation increases the reactiv

90 nstrated that the molecular structure of the MnP catalyst was retained.

91 high- to low-spin transition for all of the MnP proteins.

92 Of the MnPs tested, MnT4MPyP exerted the greatest effect on inc

93 nally, we combined the light-protected TiO2 |MnP cathode with a CdS-sensitized photoanode to enable s

94 er of 112+/-17 was attained with these TiO2 |MnP electrodes after 2 h electrolysis.

95 Both materials exhibit a rocksalt-to-MnP phase transition under compression with ca. 22 % uni

96 w-spin heme species for native and wild-type MnP and show that the location of the engineered disulfi

97 In comparison to wild-type MnP, enzymes containing engineered disulfide bonds in th

98 o the corresponding values for the wild-type MnP.

99 ately 300-fold lower than that for wild-type MnP.

100 slower rates of inactivation than wild-type MnP.

101 oximately 22-fold greater than for wild-type MnP.

102 the R177A and R177K MnPs than for wild-type MnP.

103 proximately 10-fold lower than for wild-type MnP.

104 n the corresponding k(cat) for the wild-type MnP.

105 on were similar for the mutant and wild-type MnPs.

106 I) were similar for the mutant and wild-type MnPs.

107 The manganese peroxidase variants (MnPs) were purified and characterized by kinetic and spe

108 oordinate, high-spin heme at pH 9.0, whereas MnP with multiple engineered disulfide bonds did not exh

109 , which harbors many white-rot taxa, whereas MnPs and VPs are more widespread and may have multiple o

110 As with MnP, the activity of MnCcP(W51F, W191F) was found to inc