title: Dissecting the mechanism of oxygen trafficking in a metalloenzyme.
abstract: A key question in the biological activation of oxygen is how the protein matrix regulates the delivery of oxygen to its site of activation. We are using Escherichia coli copper amine oxidase as a model system to investigate the roles played by both local active site residues as well as long range interactions in this process. We have generated active site mutants, as well as mutants in the putative oxygen delivery channel and characterised their affects on enzyme structure and catalysis.
authors.affiliation: Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Smith
authors.forename: Peter F
authors.initials: PF
authors.lastname: Knowles
authors.forename: Michael J
authors.initials: MJ
authors.lastname: McPherson
authors.forename: Arwen R
authors.initials: AR
authors.lastname: Pearson
mesh_terms: D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry*; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D010100:Oxygen / Q000737:chemistry*
chemical_list: D006631:Amine Oxidase (Copper-Containing); D010100:Oxygen