戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (１語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 ion at a gold microelectrode modified with a multicopper oxidase.
2 the Fe importer Ftr1 and its partner Fet3, a multicopper oxidase.
3  the O-O bond is coupled to rapid IET in the multicopper oxidases.
4  for the evolution of nitrite reductases and multicopper oxidases.
5 ation more closely resemble the three-domain multicopper oxidases.
6 termediates in the evolution of three-domain multicopper oxidases.
7  Iron remains bound to Fpn in the absence of multicopper oxidases.
8 utative protein possessing two signatures of multicopper oxidases.
9 e different ceruloplasmins relative to other multicopper oxidases.
10 ows high sequence and functional homology to multicopper oxidases.
11 resent evidence that Drosophila melanogaster multicopper oxidase-1 (MCO1) is a functional ferroxidase
12 four components involved in iron absorption: Multicopper oxidase-4 (Mco4), a Fet3p ortholog, is essen
13 no acid sequence similarity to the family of multicopper oxidases, a diverse group of proteins that u
14 n by an enzyme or enzyme complex involving a multicopper oxidase, although the biochemical mechanism
15 ultiple auxiliary metabolic genes, including multicopper oxidases and ammonia monooxygenase subunit C
16 This copper atom is not present in any other multicopper oxidase, and its presence appears to stabili
17                                          The multicopper oxidases are a family of enzymes that couple
18                               The two-domain multicopper oxidases are proposed to be key intermediate
19    LACCASEs, a family of cell wall-localized multicopper oxidases, are involved in lignin biosynthesi
20 uel cell, termed "BioBattery", that utilizes multicopper oxidases as the anodic enzyme in a non-diffu
21 er in an enzymatic fuel cell together with a multicopper oxidase at the cathode, or in a proton excha
22                                          The multicopper oxidases catalyze the 4e- reduction of O2 to
23                                              Multicopper oxidases catalyze the 4e- reduction of O2 to
24                                          The multicopper oxidases contain at least four copper atoms
25                         The Escherichia coli multicopper oxidase copper efflux oxidase (CueO) is part
26  that support a hypothesis that the putative multicopper oxidase CueO and the transenvelope transport
27                                          The multicopper oxidase CueO had previously been demonstrate
28                                          The multicopper oxidase CueO oxidizes toxic Cu(I) and is req
29                     We further show that the multicopper oxidase encoded by LOW PHOSPHATE ROOT 1 (LPR
30  proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a per
31 ntiserum was generated against hephaestin, a multicopper oxidase essential for enteric iron absorptio
32                Human ceruloplasmin (CP) is a multicopper oxidase essential for normal iron homeostasi
33                           Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasi
34       Based on FET3 sequence homology to the multicopper oxidase family and iron oxidation studies in
35              This protein is a member of the multicopper oxidase family, an evolutionarily conserved
36       Bilirubin oxidases, a sub class of the Multicopper oxidases family, were discovered in 1981 by
37                                          The multicopper oxidase Fet3p catalyzes the four-electron re
38                                          The multicopper oxidase Fet3p couples four 1e(-) oxidations
39 s to import iron, but yeasts also employ the multicopper oxidase Fet3p for high-affinity iron uptake
40                                          The multicopper oxidase Fet3p is thought to convert extracel
41 isiae restored copper incorporation into the multicopper oxidase Fet3p, providing direct evidence of
42 tant abrogated copper incorporation into the multicopper oxidase Fet3p.
43 restoration of copper incorporation into the multicopper oxidase Fet3p.
44 ort system, which relies on the cell surface multicopper oxidase Fet3p.
45 visiae, Fe(II) is oxidized to Fe(III) by the multicopper oxidase, Fet3p, and the Fe(III) produced is
46                                  These are a multicopper oxidase, Fet3p, with specificity towards Fe(
47  of blue copper oxidase, a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been
48                     The optimal pairing used multicopper oxidase from Pyrobaculum aerophilum as the a
49 ious enzyme variants as the anode, including multicopper oxidase from Pyrobaculum aerophilum, laccase
50 nducible oxidase activity, attributed to the multicopper oxidase function of PcoA.
51                       A number of two-domain multicopper oxidases have been identified from genome se
52  of the metal transporter IREG1/MTP1 and the multicopper oxidase, hephaestin.
53 s fatty acid desaturase homolog (Ole2) and a multicopper oxidase homolog (Fet3) play roles in prostag
54 his is consistent with a possible role for a multicopper oxidase in Arabidopsis Fe homeostasis, as pr
55                                   Fet3p is a multicopper oxidase in this membrane essential for high
56            Ceruloplasmin is unique among the multicopper oxidases in that in addition to the usual co
57 ) process supports a molecular mechanism for multicopper oxidases in which O(2) is reduced to H(2)O i
58 xide-responsive transcriptional regulator, a multicopper oxidase involved in denitrification, and an
59 zation of Ctr1p (copper transporter), Fet3p (multicopper oxidase involved in high-affinity iron uptak
60 tion of O2 at the trinuclear active sites of multicopper oxidases is discussed.
61                               CueO (YacK), a multicopper oxidase, is part of the copper-regulatory cu
62                             Here, we explore multicopper oxidases (laccases) as a new enzyme class fo
63 cs model for catalytic dioxygen reduction on multicopper oxidase (MCO) cathodes.
64 dants, but others can use O(2) directly, via multicopper oxidase (MCO) enzymes.
65                                       A CotA multicopper oxidase (MCO) from Bacillus pumilus, previou
66 s to find genes encoding ferroxidases of the multicopper oxidase (MCO) gene family in an attempt to i
67 hyrin (ZnTMPyP(4+)) photosensitizer with the multicopper oxidase (MCO) laccase allows to link the oxi
68                                            A multicopper oxidase (MCO) MnxG protein from marine Bacil
69 The bacterial protein complex Mnx contains a multicopper oxidase (MCO) MnxG that, unusually, catalyze
70 e function at the root tip revealed multiple multicopper oxidase (MCO) proteins, such as Fe-responsiv
71                  The enzyme mechanism of the multicopper oxidase (MCO) SLAC from Streptomyces coelico
72     Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) that contains 3 cupredoxin-lik
73                                   Fet3p is a multicopper oxidase (MCO) that functions together with t
74 ction in Aspergillus nidulans identified the multicopper oxidase (MCO) VdtB responsible for the regio
75            A gene (yacK) encoding a putative multicopper oxidase (MCO) was cloned from Escherichia co
76 ) genes, including mnxG, encoding a putative multicopper oxidase (MCO), as responsible for this two-e
77 s sp. PL-12, Mnx, is a complex composed of a multicopper oxidase (MCO), MnxG, and two accessory prote
78 f manganese solid formation (as MnOx) by the multicopper oxidase (MCO)-containing Mnx protein complex
79                               High-potential multicopper oxidases (MCOs) are excellent catalysts able
80                                          The multicopper oxidases (MCOs) are the family of enzymes th
81 estigated the role of the enzymatic group of multicopper oxidases (MCOs) as one putatively relevant d
82                                              Multicopper oxidases (MCOs) catalyze the 4e(-) reduction
83                                              Multicopper oxidases (MCOs) catalyze the oxidation of a
84                                          The multicopper oxidases (MCOs) couple four 1e(-) oxidations
85 e of expensive and inefficient Pt catalysts, multicopper oxidases (MCOs) have been envisioned because
86                               High potential multicopper oxidases (MCOs) have T1 reduction potentials
87 G of the Mnx protein complex is unique among multicopper oxidases (MCOs) in carrying out a two-electr
88                                          The multicopper oxidases (MCOs) utilize a blue type 1 (T1) c
89                                              Multicopper oxidases (MCOs) utilize a tricopper active s
90                                              Multicopper oxidases (MCOs) utilize an electron shuttlin
91 n hemocyanin (Hc), tyrosinase (Tyr), and the multicopper oxidases (MCOs), such as laccase (Lc), and p
92 road agreement on the catalytic mechanism of multicopper oxidases (MCOs), the geometric and electroni
93                                           In multicopper oxidases (MCOs), the type 1 (T1) Cu accepts
94 rmediate Cu(II)Cu(II)Cu(II)(mu(3)-O) (NI) in multicopper oxidases (MCOs).
95  (NiRs) and the trinuclear Cu cluster in the multicopper oxidases (MCOs).
96 . tuberculosis and was renamed mycobacterial multicopper oxidase (MmcO).
97 nsfer processes, both requiring the putative multicopper oxidase, MnxG, in which Mn(III) is a transie
98 ion, purification, and characterization of a multicopper oxidase, Nmar_1354, from the AOA Nitrosopumi
99                          Hence, Rv0846c is a multicopper oxidase of M. tuberculosis and was renamed m
100 rprising role in stabilizing the periplasmic multicopper oxidase PcoA, encoded within the same operon
101                                          The multicopper oxidase phenoxazinone synthase (PHS) catalyz
102                                   Fet3p is a multicopper oxidase recently isolated from the yeast, Sa
103               This is the highest resolution multicopper oxidase structure yet determined and provide
104          SufI is structurally related to the multicopper oxidase superfamily but lacks metal cofactor
105 ing that the reaction might involve a unique multicopper oxidase system capable of a two-electron oxi
106 dation of Mn(II) appears to involve a unique multicopper oxidase system capable of the overall two-el
107                                 Laccase is a multicopper oxidase that contains four Cu ions, one type
108                                 Laccase is a multicopper oxidase that contains four Cu ions, one type
109                                   Fet3p is a multicopper oxidase that contains four Cu ions: one type
110                             CueO itself is a multicopper oxidase that requires copper for activity.
111                                   Fet3p is a multicopper oxidase that uses four copper ions (one type
112 t with that of human ceruloplasmin and other multicopper oxidases that are devoid of ferroxidase acti
113                            Laccases are blue multicopper oxidases that catalyse the four-electron red
114 the unique reactivity of this and homologous multicopper oxidases that support the essential traffick
115 t ectoine and an unprecedented enrichment of multicopper oxidases, thioredoxin-like proteins, and tra
116 ne of the predicted gene products encoding a multicopper oxidase to validate the screen.
117  energies of the type 1 (T1) Cu site in four multicopper oxidases were calculated by combining first
118 3 protein from Saccharomyces cerevisiae is a multicopper oxidase with specificity toward Fe(II) and C
119 ion of the type 1 Cu sites of four different multicopper oxidases with two different substrates were

 
Page Top