MONOAMINE-OXIDASE CONTAINS A REDOX-ACTIVE DISULFIDE

Mitochondrial monoamine oxidases A and B (MAO A and MAO B) are ubiquit ous homodimeric FAD-containing oxidases that catalyze the oxidation of biogenic amines. Both enzymes play a vital role in the regulation of neurotransmitter levels in brain and are of interest as drug targets. However, little is known about the amino acid residues involved in the catalysis. The experiments reported here show that both MAO A and MAO B contain a redox-active disulfide at the catalytic center. The resul ts imply that MAO may be a novel type of disulfide oxidoreductase and open the way to characterizing the catalytic and chemical mechanism of the enzyme.