Dopamine-β-hydroxylase: Evidence for binuclear copper sites

Ninian J. Blackburn, Howard S. Mason, Peter F. Knowles

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

Copper has been progressively removed from dopamine-β-hydroxylase by incubation with chelex resin. The relationship between the activity (A) and the copper/protein ratio (r) has been shown to be of the form Ar2 which implies that the enzyme catalysed reaction is second order with respect to protein bound copper. These results support a model for the catalytic mechanism involving binuclear copper sites rather than the four copper atoms in the enzyme acting independently.

Original languageEnglish (US)
Pages (from-to)1275-1281
Number of pages7
JournalTopics in Catalysis
Volume95
Issue number3
DOIs
StatePublished - Jan 1 1980

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Dopamine-β-hydroxylase: Evidence for binuclear copper sites'. Together they form a unique fingerprint.

  • Cite this