Pages that link to "Q58233452"
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The following pages link to Spectroscopic and Kinetic Studies on the Oxygen-centered Radical Formed during the Four-electron Reduction Process of Dioxygen byRhus verniciferaLaccase (Q58233452):
Displaying 19 items.
- Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties (Q27640698) (← links)
- Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis (Q27643087) (← links)
- An O-centered structure of the trinuclear copper center in the Cys500Ser/Glu506Gln mutant of CueO and structural changes in low to high X-ray dose conditions (Q27676773) (← links)
- Copper active sites in biology (Q28658988) (← links)
- Primary structure of a Japanese lacquer tree laccase as a prototype enzyme of multicopper oxidases (Q30837183) (← links)
- O2 reduction to H2O by the multicopper oxidases (Q33787004) (← links)
- Mechanism of the reduction of the native intermediate in the multicopper oxidases: insights into rapid intramolecular electron transfer in turnover (Q34926987) (← links)
- Two-Electron Reduction versus One-Electron Oxidation of the Type 3 Pair in the Multicopper Oxidases (Q35858726) (← links)
- The two oxidized forms of the trinuclear Cu cluster in the multicopper oxidases and mechanism for the decay of the native intermediate (Q35962932) (← links)
- Functional expression of a fungal laccase in Saccharomyces cerevisiae by directed evolution. (Q39708642) (← links)
- Electronic structure of the peroxy intermediate and its correlation to the native intermediate in the multicopper oxidases: insights into the reductive cleavage of the o-o bond (Q41824849) (← links)
- Molecular origin of rapid versus slow intramolecular electron transfer in the catalytic cycle of the multicopper oxidases (Q41871658) (← links)
- Four-electron reduction of dioxygen by a multicopper oxidase, CueO, and roles of Asp112 and Glu506 located adjacent to the trinuclear copper center. (Q41914201) (← links)
- New insights into the catalytic active-site structure of multicopper oxidases (Q43480179) (← links)
- Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity (Q51662283) (← links)
- Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen. (Q54460435) (← links)
- A new chiral, poly-imidazole N8-ligand and the related di- and tri-copper(ii) complexes: synthesis, theoretical modelling, spectroscopic properties, and biomimetic stereoselective oxidations (Q58233404) (← links)
- Authentic and recombinant bilirubin oxidases are in different resting forms (Q73592072) (← links)
- Textile Dye Decolorizing Synechococcus PCC7942 Engineered With CotA Laccase (Q90543339) (← links)