cueO Antibody

1. Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO has been presented. PMID: 27710945
2. Exogenous acetate ion reaches the type II copper center in CueO through the water-excretion channel and potentially affects the enzymatic activity. PMID: 27380373
3. the binding of copper to apo-CueO greatly stabilized the protein, indicating a transformation from an open or flexible domain arrangement with accessible copper sites to a closed structure with deeply buried copper ions. PMID: 27129241
4. The results provides evidence that CueO possesses high Mn(II) oxidase activity and generates biogenic Mn oxide gamma-Mn3O4. PMID: 24699422
5. At low levels of X-ray exposure, unambiguous electron density for an O atom is observed inside the trinuclear copper center (TNC); binding of oxygen to the TNC after its full reduction is observed in the case of the laccase. PMID: 24598746
6. Laccase activities of CueO were maximally enhanced 140-fold by virtue of the synergistic effect of mild mutations at and at around the ligand groups to type I copper. PMID: 23337502
7. These results exerted on the hydrogen bond network in CueO are discussed in comparison with proton transfers in cytochrome oxidase. PMID: 22564733
8. The results revealed that the crude CueO catalyzed the oxidation of anthracene and benzo[a]pyrene in the same way as the fungal laccase from Trametes versicolor, but showed specific characteristics such as thermostability and copper dependence. PMID: 21120471
9. has robust cuprous oxidase activity which is central to the mechanism by which CueO protects E coli against copper toxicity PMID: 15516598
10. Copper toxicity towards a cueO mutant could be suppressed by addition of the superoxide quencher 1,2-dihydroxybenzene-3,5-disulfonic acid (tiron), suggesting that a primary cause of copper toxicity is the copper-catalyzed production of superoxide anions. PMID: 15708004
11. Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. PMID: 17635554
12. Data indicate that the methionine-rich alpha-helices of CueO function as a barrier to the access of bulky organic substrates, which provides CueO with specificity as a cuprous oxidase. PMID: 17804014

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KEGG: ecj:JW0119

STRING: 316385.ECDH10B_0103