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1 ream of yacK, which encodes a putative multi-copper oxidase.
2 for redox-regulated proton transfer in heme-copper oxidases.
3 ily of enzymes that includes all of the heme-copper oxidases.
4 absolutely conserved in all other known heme-copper oxidases.
5 s (YH) moiety at the active site of the heme-copper oxidases.
6 diverged members of the superfamily of heme/copper oxidases.
7 C(epsilon) Tyr) biring structure in the heme-copper oxidases.
8 ng) is critical for the function of the heme copper oxidases.
9 types of Cu(II) sites found in multinuclear copper oxidases.
10 ext of the proton pump mechanism of the heme-copper oxidases.
11 phodiesterases (6), phytocyanins (25), multi-copper oxidases (2), extensins (6), plasma membrane rece
13 hydroxyl group of heme o in modulating heme-copper oxidase activity through participation in an extr
14 the product of this gene may function like a copper oxidase and that it may be directly responsible f
15 e later stages of dioxygen reduction in heme-copper oxidases and show that E286 is an important compo
16 t NOR is indeed structurally related to heme-copper oxidases and that it contains a heme/non-heme iro
17 rved copper binding motifs characteristic of copper oxidases, and no enzymatic function could be assi
19 ochondria and many aerobic prokaryotes, heme-copper oxidases are the terminal enzymes that couple the
21 te that cytochrome bd oxidases like the heme-copper oxidases break the O-O bond in a single four-elec
23 mental iron uptake system orthologous to the copper oxidase-dependent Fe(III) uptake system of Saccha
24 is a member of the family of radical-coupled copper oxidases, enzymes containing a free radical coord
25 showed significant similarity to other blue copper oxidases, especially with respect to the copper-b
26 The Fet3 protein (Fet3p) is a multinuclear copper oxidase essential for high-affinity iron uptake i
32 metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzy
33 probe the role of copper and protons in heme-copper oxidase (HCO), we have performed kinetic studies
38 of Fe2+ to Fe3+, by identification of yeast copper oxidases homologous to Cp that facilitate high af
40 to produce a stable peroxide intermediate in copper oxidases in which the full complement of copper a
41 ith crystallographic structural data of heme-copper oxidases, indicate that R481 plays a keystone rol
44 Although the overall architecture of blue copper oxidase is similar to nitrite reductases, detaile
45 nd dynamics of the ligand channel(s) in heme-copper oxidases is critical for understanding how the pr
47 the redox-linked enzymatic reactions of heme-copper oxidases, probably because of their different bin
48 nces of the homologous subunit in other heme-copper oxidases shows that this residue is virtually tot
50 quinol oxidases that are members of the heme-copper oxidase superfamily have a homologous subunit II,
52 hrome cbb3 oxidases are members of the haeme-copper oxidase superfamily that are important for energy
53 e c oxidase (cbb(3)-Cox) belongs to the heme-copper oxidase superfamily, and its subunits are encoded
54 ermophilus, two distinct members of the heme-copper oxidase superfamily, were immobilized on electrod
56 fungal enzyme galactose oxidase is a radical copper oxidase that catalyzes the oxidation of a broad r
57 longs to the superfamily of respiratory heme-copper oxidases that couple the reduction of molecular o
62 ndings strongly suggest that all of the heme-copper oxidases utilize the same catalytic mechanism and
63 secondary hydroxyl group of heme a/o in heme-copper oxidases, we incorporated Fe(III)-2,4 (4,2) hydro
64 herichia coli is one of the respiratory heme-copper oxidases which catalyze the reduction of O2 to wa
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