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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 erlotinib, and O-didesmethylerlotinib to the molybdenum cofactor.
10 n of nitrite to NO through reaction with its molybdenum cofactor.
11 s the electron transfer from the heme to the molybdenum cofactor.
12 ases and related compounds that requires the molybdenum cofactor.
13 tribution to the binding of sulfite near the molybdenum cofactor.
14                          Biosynthesis of the molybdenum cofactor, a chelate of molybdenum or tungsten
15 bition of electron transfer reactions at the molybdenum cofactor accounts for OA-NO2-induced inhibiti
16 mechanism is proposed for SDH, involving its molybdenum cofactor and c-type heme.
17 s the bis(molybdopterin guanine dinucleotide)molybdenum cofactor and catalyzes the reduction of D-bio
18 ction), and iron-regulated genes, as well as molybdenum cofactor and Fe-S cluster biosynthesis factor
19 he hinge 1 region of NR, which separates the molybdenum cofactor and heme domains, were specifically
20  sulfur transfer for the biosynthesis of the molybdenum cofactor, and for the thiolation of tRNA.
21 itecture, amino acid conservation around the molybdenum cofactor, and reactivity.
22     It is suggested that the haem and pterin molybdenum cofactor are associated with the 94-kDa subun
23 nformational changes near the catalytic iron-molybdenum cofactor are correlated with the nucleotide-h
24 brane is involved in iron-sulfur cluster and molybdenum cofactor assembly in the cytosol, but the tra
25      The amino acid consensus sequence for a molybdenum cofactor binding site is in HbaC.
26 herichia coli MoeA and MogA are required for molybdenum cofactor biosynthesis and are believed to fun
27 ization of proteins at inhibitory receptors, molybdenum cofactor biosynthesis and other diverse funct
28 the transfer of persulfide sulfur in humans, molybdenum cofactor biosynthesis and tRNA thiolation.
29 itric acid cycle genes in Burkholderiales or molybdenum cofactor biosynthesis genes in several phyla.
30                                              Molybdenum cofactor biosynthesis is an evolutionarily co
31 ABCDE operon coding for proteins involved in molybdenum cofactor biosynthesis is increased under aero
32 r in the genes encoding proteins involved in molybdenum cofactor biosynthesis or in the sulfite oxida
33 gh the action of two enzymes, MoaA and MoaC (molybdenum cofactor biosynthesis protein A and C, respec
34  and MoeW, enzymes involved in cell wall and molybdenum cofactor biosynthesis, respectively, as targe
35 A are required in vivo for the final step of molybdenum cofactor biosynthesis, the addition of the mo
36                            The first step in molybdenum cofactor biosynthesis, the conversion of 5'-G
37 MoaC proteins catalyze the first step during molybdenum cofactor biosynthesis, the conversion of a gu
38 ncert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guan
39  50%, showing that TusA is not essential for molybdenum cofactor biosynthesis.
40 a guanosine derivative to precursor Z during molybdenum cofactor biosynthesis.
41  8 are known to be present in humans: MOCS1, molybdenum cofactor biosynthesis; LIAS, lipoic acid bios
42 xy-scyllo-inosamine dehydrogenase (BtrN) and molybdenum cofactor biosynthetic enzyme (MoaA).
43 ral other radical SAM enzymes, including the molybdenum cofactor biosynthetic enzyme MoaA and the RNA
44 llow AdoMet radical dehydrogenase anSME, and molybdenum cofactor biosynthetic enzyme MoaA provides su
45 rsion of precursor Z to molybdopterin in the molybdenum cofactor biosynthetic pathway, are spe-cified
46 tial atom in the [MoFe7S9X] core of the iron-molybdenum cofactor cluster of nitrogenase.
47 om Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine
48                Anaerobic Salmonella uses the molybdenum cofactor-containing DmsABC enzymatic complex
49 localized in the linker between the heme and molybdenum cofactor-containing domains.
50  recently discovered as the fifth eukaryotic molybdenum cofactor-containing enzyme.
51           We establish that a predicted heme-molybdenum cofactor-containing protein, and a complex po
52                                              Molybdenum-cofactor-containing enzymes catalyze the tran
53 d spectroscopic properties, four families of molybdenum-cofactor-containing enzymes have been identif
54 e site structure and catalytic mechanisms of molybdenum-cofactor-containing enzymes.
55                                          The molybdenum cofactor contains a tricyclic pyranopterin, t
56                                              Molybdenum cofactor deficiency (MoCD) is an autosomal re
57                                              Molybdenum cofactor deficiency (MoCD) is characterised b
58 ype resembled that of humans with hereditary molybdenum cofactor deficiency and hyperekplexia (a fail
59 s in the human ortholog of MoaA that lead to molybdenum cofactor deficiency, a usually fatal disease
60 scribe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase Mo
61      It has been presumed that immature iron-molybdenum cofactor-deficient nitrogenase MoFe proteins
62                               Restoration of molybdenum cofactor-dependent enzyme activities results
63         Sulfite oxidizing enzymes (SOEs) are molybdenum cofactor-dependent enzymes that are found in
64 a controlling influence on the activity of a molybdenum cofactor enzyme.
65 is required for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) and for the maturation of
66 arries two complex metalloclusters, the iron-molybdenum cofactor (FeMo-co) and the [8Fe-7S] P-cluster
67 dinitrogen to ammonium and contains the iron-molybdenum cofactor (FeMo-co) at its active site.
68 r to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in matura
69                                         Iron-molybdenum cofactor (FeMo-co) biosynthesis involves the
70 enase maturation, having a dual role as iron-molybdenum cofactor (FeMo-co) carrier and as chaperone t
71 The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo,
72 nitrogenase active site contains an iron and molybdenum cofactor (FeMo-co) composed of 7Fe-9S-Mo-homo
73  the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized apod
74                 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was inves
75                                     The iron-molybdenum cofactor (FeMo-co) of nitrogenase contains mo
76 me of the steps for the assembly of the iron-molybdenum cofactor (FeMo-co) of nitrogenase take place.
77                 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was investi
78 iate on the biosynthetic pathway to the iron molybdenum cofactor (FeMo-co) of nitrogenase.
79 EN for further modification to form the iron-molybdenum cofactor (FeMo-co) of nitrogenase.
80 s a dinitrogen bound to the active-site iron-molybdenum cofactor (FeMo-co) of the nitrogenase MoFe pr
81 e also involved in the synthesis of the iron-molybdenum cofactor (FeMo-co) of the widely studied moly
82 factor Y) is able to bind either to the iron molybdenum cofactor (FeMo-co) or to apodinitrogenase and
83 dinitrogenase, NifH is required for the iron-molybdenum cofactor (FeMo-co) synthesis and apodinitroge
84 tant is routinely added to the in vitro iron-molybdenum cofactor (FeMo-co) synthesis assay, although
85 S = 1/2 EPR signal from the active-site iron-molybdenum cofactor (FeMo-co) to which are bound at leas
86 FH functions in the biosynthesis of the iron-molybdenum cofactor (FeMo-co), and in the processing of
87                                     The iron-molybdenum cofactor (FeMo-co), located at the active sit
88 plex metal cofactors known to date, the iron-molybdenum cofactor (FeMo-co).
89 N2 at the [Fe7, Mo, S9, X, homocitrate] iron-molybdenum cofactor (FeMo-co).
90  contains a P cluster ([8Fe-7S]) and an iron-molybdenum cofactor (FeMoco) ([Mo-7Fe-9S-X-homocitrate])
91   The structures of the protein and the iron-molybdenum cofactor (FeMoco) appear to be largely unaffe
92                However, its function in iron-molybdenum cofactor (FeMoco) biosynthesis has not been c
93 ective in its ability to participate in iron-molybdenum cofactor (FeMoco) insertion.
94                                      An iron-molybdenum cofactor (FeMoco) is thought to be the site o
95 titial carbon atom at the center of the iron-molybdenum cofactor (FeMoco) of MoFe-nitrogenase, its ro
96                                     The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a b
97                       The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the large
98 n centers purportedly accumulate on the iron-molybdenum cofactor (FeMoco) of nitrogenase, and their r
99 ntaining iron-sulfur cluster called the iron-molybdenum cofactor (FeMoco).
100 lasmic side of the membrane and contains one molybdenum cofactor, five [Fe-S] clusters, and one heme
101  a labile selenium cofactor in addition to a molybdenum cofactor, flavin adenine dinucleotide, and Fe
102 us and require a prosthetic group called the molybdenum cofactor for activity.
103 um species which is used in the synthesis of molybdenum cofactor from Mo-free molybdopterin.
104 cess involves oxidation of the pterin of the molybdenum cofactor from the tetrahydro to a dihydro oxi
105 een used to investigate the structure of the molybdenum cofactor in DMSO reductase from Rhodobacter c
106 n the NuoG subunit resembles the GTP-derived molybdenum cofactor in homologous formate dehydrogenase
107 f the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl
108                                          The molybdenum cofactor is an important cofactor, and its bi
109 FdhD contains both metal centers, albeit the molybdenum cofactor is at a reduced level.
110                                          The molybdenum cofactor is ubiquitous in nature, and the pat
111 scopically distinct [2Fe-2S] clusters, and a molybdenum cofactor located within the protein active si
112 plant cells, independent of ABA3 function in molybdenum cofactor maturation.
113  nitrogenases in addition to nif genes for a molybdenum cofactor (Mo) nitrogenase.
114 nd in proteins to a pterin, thus forming the molybdenum cofactor (Moco) at the catalytic sites of mol
115 am of genes encoding molybdate transporters, molybdenum cofactor (Moco) biosynthesis enzymes, and pro
116                                              Molybdenum cofactor (Moco) biosynthesis is a highly cons
117                                              Molybdenum cofactor (Moco) biosynthesis is an evolutiona
118  revealed that PA1006 interacts with several molybdenum cofactor (MoCo) biosynthesis proteins as well
119  coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis, an evolutionari
120 Here, using MoaA, aradical SAM enzyme in the molybdenum cofactor (Moco) biosynthesis, as a model, we
121 cyclo-7,8-dihydro-GTP (3',8-cH(2)GTP) in the molybdenum cofactor (Moco) biosynthesis.
122 o-7,8-dihydro-GTP (3',8-cH(2)GTP) during the molybdenum cofactor (Moco) biosynthesis.
123                                          The molybdenum cofactor (Moco) consists of a unique and cons
124  to the DMSO reductase (DMSOR) family of the molybdenum cofactor (Moco) containing enzymes and cataly
125 malonic encephalopathy protein 1 (ETHE1) and molybdenum cofactor (MoCo) deficiencies are hereditary d
126        We have shown previously that lack of molybdenum cofactor (MoCo) in Escherichia coli leads to
127 d activities of several enzymes that require molybdenum cofactor (MoCo) in vp15 mutant seedlings.
128                                              Molybdenum cofactor (Moco) is a prosthetic group necessa
129                                          The molybdenum cofactor (Moco) is a redox cofactor found in
130                                          The molybdenum cofactor (Moco) is an essential redox cofacto
131                                          The molybdenum cofactor (Moco) is essential for all kingdoms
132                                          The molybdenum cofactor (Moco) is found in a variety of enzy
133                                          The molybdenum cofactor (Moco) is found in the active site o
134            Xanthine dehydrogenase (XDH) is a molybdenum cofactor (Moco) requiring enzyme that catabol
135                                 The heme and molybdenum cofactor (Moco) subunits are tightly associat
136 sed cloning reveals that LOS5/ABA3 encodes a molybdenum cofactor (MoCo) sulfurase.
137 (MPT)-free sulfite oxidase in vitro with the molybdenum cofactor (Moco) synthesized de novo from prec
138 iring the synthesis of the sulfur-containing molybdenum cofactor (MoCo), and (iii) the thiolation of
139  riboswitches was proposed to respond to the molybdenum cofactor (Moco), which serves as a redox cent
140 s bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants
141 ing normal function of molybdenum enzymes in molybdenum cofactor (MoCo)-deficient mice and human pati
142          Nitrate reductase (NR) is a complex molybdenum cofactor (Moco)-dependent homodimeric metallo
143  lacked additional activities that require a molybdenum cofactor (Moco).
144 nd the pterin moiety form the redox reactive molybdenum cofactor (Moco).
145 metabolism of these compounds depends on the molybdenum cofactor (MoCo).
146 ynthesis of the transcription factor FNR, in molybdenum cofactor (molybdopterin guanine dinucleotide
147                                     The iron-molybdenum cofactor of nitrogenase (FeMo-co) is synthesi
148                                     The iron-molybdenum cofactor of nitrogenase (FeMoco) catalyzes fi
149 ore, the identities of all atoms in the iron-molybdenum cofactor of nitrogenase have finally been elu
150 g to those reported for CO bound to the iron-molybdenum cofactor of nitrogenase were detected during
151 roperties of the Fe and Mo sites of the iron-molybdenum cofactor of nitrogenase with respect to bindi
152       Molybdenum, as a component of the iron-molybdenum cofactor of nitrogenase, is essential for sym
153 central Fe and terminal Mo sites of the iron-molybdenum cofactor of nitrogenase.
154 sformations that may be possible at the iron-molybdenum cofactor of nitrogenases, which may have hydr
155  inactivation of the enzyme concomitant with molybdenum cofactor release, indicating that histidine r
156                            Here we report on MOlybdenum COfactor Sulfurase (MOCOS), an enzyme involve
157 ductase (CYB5R), cytochrome b(5) (CYB5), and molybdenum cofactor sulfurase C-terminal containing 1 an
158 sphate (cPMP), requires the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1).
159 y with two proteins, MogA and MoeA, from the molybdenum cofactor synthesis pathway in E. coli, as wel
160 ybdenum is incorporated into proteins as the molybdenum cofactor that contains a mononuclear molybden
161                                     The iron-molybdenum cofactor (the M-cluster) serves as the active
162 ase 2 is also activable in vitro by the iron-molybdenum cofactor to form a hybrid enzyme with unique
163 r one-electron transfer (IET) steps from the molybdenum cofactor to the iron of the integral b-type h
164 r one-electron transfer (IET) steps from the molybdenum cofactor to the iron of the integral b-type h
165                                     The iron-molybdenum cofactor was unable to replace FeV-co in prom
166  the Fe and Mo sites of the nitrogenase iron-molybdenum cofactor with respect to the binding of H and

 
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