Work

Structural Basis for Copper–Oxygen Mediated C−H Bond Activation by the Formylglycine‐Generating Enzyme

Year: 2017

Type: article

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 Ag I or Cd II 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 Cu I/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.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.201702901

Authors: Marcel Meury, Matthias Knop, Florian P. Seebeck

Institution: University of Basel

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, European Research Council

Awards: G6310232755, Characterization and engineering of lignin:protein interactions