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Visualization of dioxygen bound to copper during enzyme catalysis
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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1999 (English)In: SCIENCE, ISSN 0036-8075, Vol. 286, no 5445, 1724-1728 p.Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
AMER ASSOC ADVANCEMENT SCIENCE , 1999. Vol. 286, no 5445, 1724-1728 p.
Keyword [en]
SERUM AMINE OXIDASE; CRYSTAL-STRUCTURE; BENZYLAMINE OXIDASE; ESCHERICHIA-COLI; HALF-REACTION; PIG PLASMA; MECHANISM; TOPAQUINONE; RESOLUTION; CRYSTALLOGRAPHY
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-84823OAI: oai:DiVA.org:uu-84823DiVA: diva2:112731
Note
Addresses: Wilmot CM, Univ Leeds, Sch Biochem & Mol Biol, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England. Univ Leeds, Sch Biochem & Mol Biol, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England. Univ Uppsala, Dept Biochem,Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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