edoc

Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme

Meury, Marcel and Knop, Matthias and Seebeck, Florian P.. (2017) Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme. Angewandte Chemie International Edition, 56 (28). pp. 8115-8119.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/58310/

Downloads: Statistics Overview

Abstract

The formylglycine-generating enzyme (FGE) is a unique copper protein that catalyzes oxygen-dependent C-H activation. We describe 1.66 Å- and 1.28 Å-resolution crystal structures of FGE from Thermomonospora curvata in complex with either AgI or CdII providing definitive evidence for a high-affinity metal-binding site in this enzyme. The structures reveal a bis-cysteine linear coordination of the monovalent metal, and tetrahedral coordination of the bivalent metal. Similar coordination changes may occur in the active enzyme as a result of CuI/II redox cycling. Complexation of copper atoms by two cysteine residues is common among copper-trafficking proteins, but is unprecedented for redox-active copper enzymes or synthetic copper catalysts.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Molecular Bionics (Seebeck)
UniBasel Contributors:Seebeck, Florian Peter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:1433-7851
e-ISSN:1521-3773
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:05 Jan 2018 13:48
Deposited On:05 Jan 2018 13:48

Repository Staff Only: item control page