Abstract
Tryptophan and tyrosine residues in proteins may be posttranslationally modified to form enzyme cofactors. Tryptophan tryptophylquinone (TTQ), the cofactor of methylamine dehydrogenase (MADH), is formed by covalent cross-linking of two tryptophan residues and incorporation of two oxygen atoms into one of the indole rings to form a quinone. MADH converts primary amines to their corresponding aldehydes plus ammonia. During the catalytic cycle, TTQ mediates electron transfer from substrate to a copper protein, amicyanin. These electrons are transferred to the respiratory chain via a c-type cytochrome. Structural, kinetic and site-directed mutagenesis studies have characterized protein-protein interactions, and mechanisms of catalysis and electron transfer by TTQ. Preliminary results obtained with MADH enzyme-electrodes demonstrate the potential for quinoprotein-based biosensors.
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