Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism

Dalton Trans. 2015 Feb 21;44(7):3251-8. doi: 10.1039/c4dt03010a.

Abstract

A new tridentate N-donor ligand and its corresponding copper(i) complex have been synthesized to investigate the tyrosinase-like aromatic hydroxylation of an attached phenol. The results of the oxygenation reactions are compared to related systems having attached phenyl and catechol groups, respectively. The title complex is the first system mediating the monooxygenation of a phenol in the absence of an external base.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Activation
  • Models, Chemical*
  • Monophenol Monooxygenase / chemistry*
  • Monophenol Monooxygenase / metabolism*
  • Phenol / chemistry
  • Phenol / metabolism

Substances

  • Phenol
  • Monophenol Monooxygenase