Evidence Against Reduction of Cu2+ to Cu+ during Dioxygen Activation in a Copper Amine Oxidase from Yeast
- 28 September 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (41) , 9897-9904
- https://doi.org/10.1021/ja000325f
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Visualization of Dioxygen Bound to Copper During Enzyme CatalysisScience, 1999
- An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase from Hansenula polymorphaBiochemistry, 1999
- Mutation of a Strictly Conserved, Active-Site Residue Alters Substrate Specificity and Cofactor Biogenesis in a Copper Amine OxidaseBiochemistry, 1999
- Relationship between Conserved Consensus Site Residues and the Productive Conformation for the TPQ Cofactor in a Copper-Containing Amine Oxidase from YeastBiochemistry, 1998
- Spectroscopically Distinct Cobalt(II) Sites in Heterodimetallic Forms of the Aminopeptidase from Aeromonas proteolytica: Characterization of Substrate BindingBiochemistry, 1997
- Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion‐dependent autooxidation of a specific tyrosyl residueFEBS Letters, 1994
- Properties of cobalt‐substituted bovine serum amine oxidaseEuropean Journal of Biochemistry, 1994
- Synthesis and spectroscopic characterization of model compounds for the active site cofactor in copper amine oxidasesJournal of the American Chemical Society, 1993
- Preparation and spectroscopic characterization of a coupled binuclear center in cobalt(II)-substituted hemocyaninBiochemistry, 1992
- Effect of metal substitution on the chromophore of bovine serum amine oxidaseBiochemistry, 1983