Bioinspired aerobic substrate oxidation: A Ni(II)-oximate catalyst that parallels biological alcohol and amine oxidation chemistry

Michael J. Baldwin, Jeanette A. Krause, Michael J. Goldcamp, Micheal Haven, Sara E. Edison, Leah N. Squires

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

4 Scopus citations

Abstract

The Ni(II) complex of tris(1-propan-2-onyl oximato)amine (TRISOX) catalyzes the aerobic oxidation of primary alcohols and amines. Parallels to several metalloenzymes guide studies of Ni(TRISOX) chemistry. Ni(TRISOX) catalyzes the same net reactions as galactose oxidase, Cu-dependent amine oxidase, and catalase. Spectroscopy of an observable catalytic intermediate shows reversible oxidation of ligand oximates to iminoxyl radicals. Galactose oxidase and amine oxidase also require both a redox-active organic component and a transition metal. Crystal structures of Hn TRISOX ligands with Fe, Co, Cu and Zn extend this chemistry to other metals.

Original languageEnglish
Title of host publicationBioinorganic Chemistry
Subtitle of host publicationCellular Systems and Synthetic Models
PublisherAmerican Chemical Society
Pages133-150
Number of pages18
ISBN (Print)9780841269750
DOIs
StatePublished - May 21 2009

Publication series

NameACS Symposium Series
Volume1012
ISSN (Print)0097-6156
ISSN (Electronic)1947-5918

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