Probing the radical mechanism of galactose oxidase using an ultrafast radical probe

B. Elizabeth Turner, Bruce Branchaud

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Processing of trans-2-phenylcyclopropylmethanols 5 and 6 by the monocopper/tyrosine radical enzyme galactose oxidase led to mechanism-based inactivation with a partition ratio, (k(cat) + k(inact))/k(inact), of approximately 1 and a primary deuterium isotope effect, k(inact(H))/k(inact(D)), of 3.2. The data are consistent with a radical mechanism for galactose oxidase with a short lived ketyl radical anion intermediate.

Original languageEnglish (US)
Pages (from-to)3341-3346
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Volume9
Issue number23
DOIs
StatePublished - Dec 6 1999
Externally publishedYes

Fingerprint

Galactose Oxidase
Deuterium
Isotopes
Anions
Enzymes
Processing

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

Cite this

Probing the radical mechanism of galactose oxidase using an ultrafast radical probe. / Turner, B. Elizabeth; Branchaud, Bruce.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 9, No. 23, 06.12.1999, p. 3341-3346.

Research output: Contribution to journalArticle

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