ライフサイエンスコーパス: molybdenum cofactor

1 ining biomolecules (e.g., thiolated tRNA and molybdenum cofactor).

2 m to the dithiolene of molybdopterin to form molybdenum cofactor.

3 n the bis(molybdopterin guanine dinucleotide)molybdenum cofactor.

4 ase demonstrated the presence of the bis(MGD)molybdenum cofactor.

5 guanine dinucleotide, the active form of the molybdenum cofactor.

6 molybdopterin during the biosynthesis of the molybdenum cofactor.

7 ed binding sites for [2Fe-2S] clusters and a molybdenum cofactor.

8 form B of the pterin component of the pterin molybdenum cofactor.

9 n of nitrite to NO through reaction with its molybdenum cofactor.

10 s the electron transfer from the heme to the molybdenum cofactor.

11 ases and related compounds that requires the molybdenum cofactor.

12 tribution to the binding of sulfite near the molybdenum cofactor.

13 Biosynthesis of the molybdenum cofactor, a chelate of molybdenum or tungsten

14 bition of electron transfer reactions at the molybdenum cofactor accounts for OA-NO2-induced inhibiti

15 mechanism is proposed for SDH, involving its molybdenum cofactor and c-type heme.

16 s the bis(molybdopterin guanine dinucleotide)molybdenum cofactor and catalyzes the reduction of D-bio

17 ction), and iron-regulated genes, as well as molybdenum cofactor and Fe-S cluster biosynthesis factor

18 he hinge 1 region of NR, which separates the molybdenum cofactor and heme domains, were specifically

19 sulfur transfer for the biosynthesis of the molybdenum cofactor, and for the thiolation of tRNA.

20 It is suggested that the haem and pterin molybdenum cofactor are associated with the 94-kDa subun

21 brane is involved in iron-sulfur cluster and molybdenum cofactor assembly in the cytosol, but the tra

22 The amino acid consensus sequence for a molybdenum cofactor binding site is in HbaC.

23 herichia coli MoeA and MogA are required for molybdenum cofactor biosynthesis and are believed to fun

24 ization of proteins at inhibitory receptors, molybdenum cofactor biosynthesis and other diverse funct

25 the transfer of persulfide sulfur in humans, molybdenum cofactor biosynthesis and tRNA thiolation.

26 itric acid cycle genes in Burkholderiales or molybdenum cofactor biosynthesis genes in several phyla.

27 Molybdenum cofactor biosynthesis is an evolutionarily co

28 ABCDE operon coding for proteins involved in molybdenum cofactor biosynthesis is increased under aero

29 r in the genes encoding proteins involved in molybdenum cofactor biosynthesis or in the sulfite oxida

30 gh the action of two enzymes, MoaA and MoaC (molybdenum cofactor biosynthesis protein A and C, respec

31 and MoeW, enzymes involved in cell wall and molybdenum cofactor biosynthesis, respectively, as targe

32 A are required in vivo for the final step of molybdenum cofactor biosynthesis, the addition of the mo

33 The first step in molybdenum cofactor biosynthesis, the conversion of 5'-G

34 MoaC proteins catalyze the first step during molybdenum cofactor biosynthesis, the conversion of a gu

35 ncert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guan

36 50%, showing that TusA is not essential for molybdenum cofactor biosynthesis.

37 a guanosine derivative to precursor Z during molybdenum cofactor biosynthesis.

38 8 are known to be present in humans: MOCS1, molybdenum cofactor biosynthesis; LIAS, lipoic acid bios

39 xy-scyllo-inosamine dehydrogenase (BtrN) and molybdenum cofactor biosynthetic enzyme (MoaA).

40 ral other radical SAM enzymes, including the molybdenum cofactor biosynthetic enzyme MoaA and the RNA

41 llow AdoMet radical dehydrogenase anSME, and molybdenum cofactor biosynthetic enzyme MoaA provides su

42 rsion of precursor Z to molybdopterin in the molybdenum cofactor biosynthetic pathway, are spe-cified

43 tial atom in the [MoFe7S9X] core of the iron-molybdenum cofactor cluster of nitrogenase.

44 om Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine

45 localized in the linker between the heme and molybdenum cofactor-containing domains.

46 recently discovered as the fifth eukaryotic molybdenum cofactor-containing enzyme.

47 We establish that a predicted heme-molybdenum cofactor-containing protein, and a complex po

48 Molybdenum-cofactor-containing enzymes catalyze the tran

49 d spectroscopic properties, four families of molybdenum-cofactor-containing enzymes have been identif

50 e site structure and catalytic mechanisms of molybdenum-cofactor-containing enzymes.

51 The molybdenum cofactor contains a tricyclic pyranopterin, t

52 Molybdenum cofactor deficiency (MoCD) is an autosomal re

53 Molybdenum cofactor deficiency (MoCD) is characterised b

54 ype resembled that of humans with hereditary molybdenum cofactor deficiency and hyperekplexia (a fail

55 s in the human ortholog of MoaA that lead to molybdenum cofactor deficiency, a usually fatal disease

56 scribe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase Mo

57 It has been presumed that immature iron-molybdenum cofactor-deficient nitrogenase MoFe proteins

58 Restoration of molybdenum cofactor-dependent enzyme activities results

59 Sulfite oxidizing enzymes (SOEs) are molybdenum cofactor-dependent enzymes that are found in

60 a controlling influence on the activity of a molybdenum cofactor enzyme.

61 is required for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) and for the maturation of

62 arries two complex metalloclusters, the iron-molybdenum cofactor (FeMo-co) and the [8Fe-7S] P-cluster

63 dinitrogen to ammonium and contains the iron-molybdenum cofactor (FeMo-co) at its active site.

64 r to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in matura

65 Iron-molybdenum cofactor (FeMo-co) biosynthesis involves the

66 enase maturation, having a dual role as iron-molybdenum cofactor (FeMo-co) carrier and as chaperone t

67 The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo,

68 nitrogenase active site contains an iron and molybdenum cofactor (FeMo-co) composed of 7Fe-9S-Mo-homo

69 the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized apod

70 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was inves

71 The iron-molybdenum cofactor (FeMo-co) of nitrogenase contains mo

72 me of the steps for the assembly of the iron-molybdenum cofactor (FeMo-co) of nitrogenase take place.

73 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was investi

74 EN for further modification to form the iron-molybdenum cofactor (FeMo-co) of nitrogenase.

75 iate on the biosynthetic pathway to the iron molybdenum cofactor (FeMo-co) of nitrogenase.

76 s a dinitrogen bound to the active-site iron-molybdenum cofactor (FeMo-co) of the nitrogenase MoFe pr

77 e also involved in the synthesis of the iron-molybdenum cofactor (FeMo-co) of the widely studied moly

78 factor Y) is able to bind either to the iron molybdenum cofactor (FeMo-co) or to apodinitrogenase and

79 dinitrogenase, NifH is required for the iron-molybdenum cofactor (FeMo-co) synthesis and apodinitroge

80 tant is routinely added to the in vitro iron-molybdenum cofactor (FeMo-co) synthesis assay, although

81 S = 1/2 EPR signal from the active-site iron-molybdenum cofactor (FeMo-co) to which are bound at leas

82 FH functions in the biosynthesis of the iron-molybdenum cofactor (FeMo-co), and in the processing of

83 The iron-molybdenum cofactor (FeMo-co), located at the active sit

84 plex metal cofactors known to date, the iron-molybdenum cofactor (FeMo-co).

85 N2 at the [Fe7, Mo, S9, X, homocitrate] iron-molybdenum cofactor (FeMo-co).

86 contains a P cluster ([8Fe-7S]) and an iron-molybdenum cofactor (FeMoco) ([Mo-7Fe-9S-X-homocitrate])

87 The structures of the protein and the iron-molybdenum cofactor (FeMoco) appear to be largely unaffe

88 However, its function in iron-molybdenum cofactor (FeMoco) biosynthesis has not been c

89 ective in its ability to participate in iron-molybdenum cofactor (FeMoco) insertion.

90 An iron-molybdenum cofactor (FeMoco) is thought to be the site o

91 titial carbon atom at the center of the iron-molybdenum cofactor (FeMoco) of MoFe-nitrogenase, its ro

92 The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a b

93 The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the large

94 n centers purportedly accumulate on the iron-molybdenum cofactor (FeMoco) of nitrogenase, and their r

95 ntaining iron-sulfur cluster called the iron-molybdenum cofactor (FeMoco).

96 lasmic side of the membrane and contains one molybdenum cofactor, five [Fe-S] clusters, and one heme

97 a labile selenium cofactor in addition to a molybdenum cofactor, flavin adenine dinucleotide, and Fe

98 us and require a prosthetic group called the molybdenum cofactor for activity.

99 um species which is used in the synthesis of molybdenum cofactor from Mo-free molybdopterin.

100 cess involves oxidation of the pterin of the molybdenum cofactor from the tetrahydro to a dihydro oxi

101 een used to investigate the structure of the molybdenum cofactor in DMSO reductase from Rhodobacter c

102 f the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl

103 The molybdenum cofactor is an important cofactor, and its bi

104 FdhD contains both metal centers, albeit the molybdenum cofactor is at a reduced level.

105 The molybdenum cofactor is ubiquitous in nature, and the pat

106 scopically distinct [2Fe-2S] clusters, and a molybdenum cofactor located within the protein active si

107 nitrogenases in addition to nif genes for a molybdenum cofactor (Mo) nitrogenase.

108 nd in proteins to a pterin, thus forming the molybdenum cofactor (Moco) at the catalytic sites of mol

109 am of genes encoding molybdate transporters, molybdenum cofactor (Moco) biosynthesis enzymes, and pro

110 Molybdenum cofactor (Moco) biosynthesis is an evolutiona

111 revealed that PA1006 interacts with several molybdenum cofactor (MoCo) biosynthesis proteins as well

112 coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis, an evolutionari

113 The molybdenum cofactor (Moco) consists of a unique and cons

114 We have shown previously that lack of molybdenum cofactor (MoCo) in Escherichia coli leads to

115 d activities of several enzymes that require molybdenum cofactor (MoCo) in vp15 mutant seedlings.

116 The molybdenum cofactor (Moco) is a redox cofactor found in

117 The molybdenum cofactor (Moco) is an essential redox cofacto

118 The molybdenum cofactor (Moco) is essential for all kingdoms

119 The molybdenum cofactor (Moco) is found in a variety of enzy

120 The heme and molybdenum cofactor (Moco) subunits are tightly associat

121 sed cloning reveals that LOS5/ABA3 encodes a molybdenum cofactor (MoCo) sulfurase.

122 (MPT)-free sulfite oxidase in vitro with the molybdenum cofactor (Moco) synthesized de novo from prec

123 iring the synthesis of the sulfur-containing molybdenum cofactor (MoCo), and (iii) the thiolation of

124 riboswitches was proposed to respond to the molybdenum cofactor (Moco), which serves as a redox cent

125 s bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants

126 ing normal function of molybdenum enzymes in molybdenum cofactor (MoCo)-deficient mice and human pati

127 Nitrate reductase (NR) is a complex molybdenum cofactor (Moco)-dependent homodimeric metallo

128 lacked additional activities that require a molybdenum cofactor (Moco).

129 nd the pterin moiety form the redox reactive molybdenum cofactor (Moco).

130 metabolism of these compounds depends on the molybdenum cofactor (MoCo).

131 ynthesis of the transcription factor FNR, in molybdenum cofactor (molybdopterin guanine dinucleotide

132 The iron-molybdenum cofactor of nitrogenase (FeMo-co) is synthesi

133 ore, the identities of all atoms in the iron-molybdenum cofactor of nitrogenase have finally been elu

134 g to those reported for CO bound to the iron-molybdenum cofactor of nitrogenase were detected during

135 roperties of the Fe and Mo sites of the iron-molybdenum cofactor of nitrogenase with respect to bindi

136 Molybdenum, as a component of the iron-molybdenum cofactor of nitrogenase, is essential for sym

137 central Fe and terminal Mo sites of the iron-molybdenum cofactor of nitrogenase.

138 sformations that may be possible at the iron-molybdenum cofactor of nitrogenases, which may have hydr

139 inactivation of the enzyme concomitant with molybdenum cofactor release, indicating that histidine r

140 Here we report on MOlybdenum COfactor Sulfurase (MOCOS), an enzyme involve

141 ductase (CYB5R), cytochrome b(5) (CYB5), and molybdenum cofactor sulfurase C-terminal containing 1 an

142 y with two proteins, MogA and MoeA, from the molybdenum cofactor synthesis pathway in E. coli, as wel

143 ybdenum is incorporated into proteins as the molybdenum cofactor that contains a mononuclear molybden

144 The iron-molybdenum cofactor (the M-cluster) serves as the active

145 ase 2 is also activable in vitro by the iron-molybdenum cofactor to form a hybrid enzyme with unique

146 r one-electron transfer (IET) steps from the molybdenum cofactor to the iron of the integral b-type h

147 r one-electron transfer (IET) steps from the molybdenum cofactor to the iron of the integral b-type h

148 The iron-molybdenum cofactor was unable to replace FeV-co in prom

149 the Fe and Mo sites of the nitrogenase iron-molybdenum cofactor with respect to the binding of H and