Premium
Structural Basis for Copper–Oxygen Mediated C−H Bond Activation by the Formylglycine‐Generating Enzyme
Author(s) -
Meury Marcel,
Knop Matthias,
Seebeck Florian P.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201702901
Subject(s) - chemistry , copper , cysteine , active site , metal , redox , enzyme , copper protein , coordination complex , stereochemistry , inorganic chemistry , organic chemistry
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.