Cu(II)-nitroxyl radicals as catalytic galactose oxidase mimics

Org Biomol Chem. 2003 Sep 21;1(18):3232-7. doi: 10.1039/b305941c.

Abstract

Results from Hammett correlation studies and primary kinetic isotope effects for the CuCl-TEMPO catalysed aerobic benzyl alcohol oxidations are inconsistent with an oxoammonium based mechanism. We postulate a copper-mediated dehydrogenation mechanism, in which TEMPO regenerates the active Cu(II)-species. This mechanism is analogous to that observed for Galactose Oxidase and mimics thereof.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohols / chemistry
  • Antioxidants / chemistry
  • Benzyl Alcohols / chemistry
  • Catalysis
  • Chemistry, Organic / methods*
  • Copper* / pharmacology
  • Cyclic N-Oxides / chemistry
  • Galactose Oxidase / chemistry*
  • Hydrogen Peroxide / pharmacology
  • Kinetics
  • Models, Chemical
  • Nitrogen Oxides / chemistry*
  • Ultraviolet Rays

Substances

  • Alcohols
  • Antioxidants
  • Benzyl Alcohols
  • Cyclic N-Oxides
  • Nitrogen Oxides
  • Copper
  • Hydrogen Peroxide
  • Galactose Oxidase
  • nitroxyl
  • cupric chloride
  • TEMPO