Abstract
The presence of pyrroloquinoline quinone at the active site of copper amine oxidases makes numerous mechanistic predictions, which include the possible formation of covalent adducts between substrate and cofactor, the transfer of nitrogen from substrate to cofactor in the reductive half of the overall reaction, and the oxidation of substrate via a proton activation mechanism. Experimental evidence in support of each of these aspects of catalysis in bovine plasma amine oxidase is presented. Direct spectroscopic evidence was also sought for initial formation of a Schiff base complex, followed by C-H bond cleavage. Rapid scanning stopped flow analysis of the anaerobic reduction of bovine plasma amine oxidase by benzylamine indicates a rapid formation of a species at 340 nm (attributed to Schiff base formation), followed by a slower decrease/increase in peaks at 480/310 nm (attributed to cofactor reduction). These findings lead to a working model for enzyme catalysis.
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© 1989 Kluwer Academic Publishers
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Klinman, J.P., Hartmann, C., Janes, S.M. (1989). Mechanistic Probes of Copper Amine Oxidases. In: Jongejan, J.A., Duine, J.A. (eds) PQQ and Quinoproteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0957-1_45
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DOI: https://doi.org/10.1007/978-94-009-0957-1_45
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