The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
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Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer.Crystal structure of an ascomycete fungal laccase from Thielavia arenaria--common structural features of asco-laccasesBilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reductionCrystal structure of the multicopper oxidase from the pathogenic bacterium Campylobacter jejuni CGUG11284: characterization of a metallo-oxidaseThe role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanismStructural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidaseCopper active sites in biologyElectron transfer and reaction mechanism of laccasesSpectroscopic and computational characterization of CuII-OOR (R = H or cumyl) complexes bearing a Me6-tren ligandBilirubin oxidase from Bacillus pumilus: a promising enzyme for the elaboration of efficient cathodes in biofuel cells.X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.Laccase engineering by rational and evolutionary design.Three-dimensional structures of laccases.μ-Bromido-bis{μ-2,2'-[4,7-diaza-decane-1,10-diylbis(nitrilo-methanylyl-idene)]diphenolato}tricopper(II) bromide dimethyl-formamide disolvate.Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase.The kinetic role of carboxylate residues in the proximity of the trinuclear centre in the O2 reactivity of CotA-laccase.The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity.
P2860
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P2860
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
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2010 nî lūn-bûn
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2010 թուականի Մարտին հրատարակուած գիտական յօդուած
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2010 թվականի մարտին հրատարակված գիտական հոդված
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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name
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@ast
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@en
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@nl
type
label
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@ast
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@en
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@nl
prefLabel
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@ast
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@en
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@nl
P2093
P50
P356
P1433
P1476
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
@en
P2093
Catarina S Silva
Peter F Lindley
Zhenjia Chen
P304
P356
10.1039/B922734B
P407
P577
2010-02-05T00:00:00Z