Dopamine β‐hydroxylase inactivation generates a protein‐bound quinone derivative
- 20 February 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 491 (1-2) , 55-58
- https://doi.org/10.1016/s0014-5793(01)02147-0
Abstract
Bovine dopamine β-hydroxylase (DbH) was inactivated by hydrogen peroxide and ascorbate in the presence of dioxygen. Both inactivated forms of the enzyme were investigated. We could highlight the presence of a quinone derivative bound to the protein, assumed as being dopa-quinone, that is absent from active enzyme. Such results suggest that a tyrosinyl radical transiently forms during catalysis. Moreover we could show that addition of substrate tyramine to H2O2 incubates is responsible for a partial protection of DbH against inactivation.Keywords
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