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Oxygen activation in a copper-containing amine oxidase
C. M. Wilmot
Chemical and Structural Biology (BMBB)
Research output
:
Contribution to journal
›
Article
›
peer-review
19
Scopus citations
Overview
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Keyphrases
Oxygen Activation
100%
Quinones
100%
Copper-containing Amine Oxidase
100%
Escherichia Coli
66%
Aldehydes
66%
Molecular Oxygen
66%
Color Change
33%
Amines
33%
Single Crystal
33%
Hydrogen Peroxide
33%
Resting State
33%
Catalytic Intermediates
33%
Steady-state Conditions
33%
Primary Amines
33%
Rate-determining Step
33%
Aerobic Conditions
33%
Anaerobic Conditions
33%
Oxidation State
33%
Two-electron
33%
H2 Formation
33%
Proton Transfer Mechanism
33%
Electron Acceptor
33%
Pre-oxidation
33%
Catalytic Turnover
33%
Dioxygen Binding
33%
Microspectrophotometry
33%
Quinoprotein
33%
Biochemistry, Genetics and Molecular Biology
Enzyme
100%
Amine Oxidase (Copper-Containing)
100%
Escherichia coli
66%
Hydrogen Peroxide
66%
Single Crystal
33%
Proton Transport
33%
Steady State
33%