Synthesis and characterization of models for cofactor biogenesis in copper amine oxidases

ORGN 38

Lawrence M. Sayre and Ke-Qing Ling. Department of Chemistry, Case Western Reserve University, Cleveland, OH 44106
The copper amine oxidases convert primary unbranched amines to aldehydes at the expense of reducing oxygen to hydrogen peroxide. The amine deamination half-reaction is mediated by one of two different quinone cofactors derived by oxidation of an active-site tyrosine, wherein either water or an active-site lysine adds to the initially formed ortho-quinone intermediate to give ultimately a 2,4,6-trihydroxyphenylalanine quinone (TPQ) or the cross-linked lysine tyrosylquinone (LTQ), respectively. Here we describe the synthesis of models with the goal of establishing chemical precedent for the overall six-electron oxidation processes needed to generate TPQ and LTQ. The LTQ model invokes an intramolecular cyclization of a pendant amine group at the ortho-quinone stage. For TPQ, since the key water addition step is proposed to involve the catalytic influence of the active site copper, the model in this case incorporates a pendant copper-coordinating ligand into the quinone precursor. Oxidation of the corresponding catechol is found to generate the TPQ-like product at neutral pH only in the presence of Cu(II).