Visualization of dioxygen bound to copper during enzyme catalysis

151Citations
Citations of this article
60Readers
Mendeley users who have this article in their library.
Get full text

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 Asp383, 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.

Cite

CITATION STYLE

APA

Wilmot, C. M., Hajdu, J., McPherson, M. J., Knowles, P. F., & Phillips, S. E. V. (1999). Visualization of dioxygen bound to copper during enzyme catalysis. Science, 286(5445), 1724–1728. https://doi.org/10.1126/science.286.5445.1724

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free