Work

The irreversible inactivation of two copper‐dependent monooxygenases by sulfite: peptidylglycine α‐amidating enzyme and dopamine β‐monooxygenase

Year: 1995

Type: article

Abstract: Peptidylglycine alpha-amidating enzyme (alpha-AE) and dopamine beta-monooxygenase (D beta M), 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 alpha-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 alpha-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 alpha-AE and D beta M most likely results from the transition metal-catalyzed oxidation of sulfite to the sulfite radical, SO3-.

Source: FEBS Letters

DOI: 10.1016/0014-5793(95)00516-c

Authors: David J. Merkler, Raviraj Kulathila, Wilson A. Francisco, David E. Ash, Joseph Bell

Institutions: University of California, Berkeley, Temple University

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: STRUCTURAL AND MECHANISTIC ANALYSIS OF LIVER ARGINASE, G2917804407, G4764320224, Structural and Mechanistic Analysis of Liver Arginase