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• W2034109636 endingPage "1728" @default.
• W2034109636 startingPage "1724" @default.
• W2034109636 abstract "X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp 383 , the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal." @default.
• W2034109636 created "2016-06-24" @default.
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• W2034109636 date "1999-11-26" @default.
• W2034109636 modified "2023-10-17" @default.
• W2034109636 title "Visualization of Dioxygen Bound to Copper During Enzyme Catalysis" @default.
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• W2034109636 doi "https://doi.org/10.1126/science.286.5445.1724" @default.
• W2034109636 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10576737" @default.
• W2034109636 hasPublicationYear "1999" @default.
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