Evidence That Dioxygen and Substrate Activation Are Tightly Coupled in Dopamine β-Monooxygenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference47 articles.
1. DOPAMINE BETA-HYDROXYLASE OF ADRENAL CHROMAFFIN GRANULES: STRUCTURE AND FUNCTION
2. Copper K-extended x-ray absorption fine structure studies of oxidized and reduced dopamine beta-hydroxylase. Confirmation of a sulfur ligand to copper(I) in the reduced enzyme.
3. The copper sites of dopamine .beta.-hydroxylase: an x-ray absorption spectroscopic study
4. Active site of dopamine .beta.-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy
5. Rapid freeze and chemical-quench studies of dopamine .beta.-monooxygenase: comparison of pre-steady-state and steady-state parameters
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