The irreversible inactivation of two copper‐dependent monooxygenases by sulfite: peptidylglycine α‐amidating enzyme and dopamine β‐monooxygenase
- 12 June 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 366 (2-3) , 165-169
- https://doi.org/10.1016/0014-5793(95)00516-c
Abstract
Peptidylglycine α-amidating enzyme (α-AE) and dopamine β-monooxygenase (DβM), two copper-dependent monooxygenases that have catalytic and structural similarities, are irreversibly inactivated by sodium sulfite in a time- and concentration-dependent manner. Studies with α-AE show that the sulfite-mediated inactivation is dependent on the presence of redox active transition metals free in solution, with Cu(II) being the most effective in supporting the inactivation reaction. Sulfite inactivation of α-AE is specific for the monooxygenase reaction of this bifunctional enzyme and amidated peptides provide protection against the inactivation. Consequently, the sulfite-mediated inactivation of α-AE and DβM most likely results from the transition metal-catalyzed oxidation of sulfite to the sulfite radical, SO3−Keywords
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