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Enzyme Research

New enzyme research reported from Johns Hopkins University

Published in Drug Week, August 24th, 2007

"A significant oxidative N-demethylation reaction occurs from a hydroperoxo-copper(II) species when formed within a tripodal tetradentate ligand framework possessing a pendant dimethylamine substrate," scientists in the United States report.

"This mimics the monoxygenase activity occurring in the copper enzyme PHM. Observation of a product-based alkoxide-Cu intermediate and determination of a reaction kinetic isotope effect (k(H)/k(D(intra)) similar to 2.3) by studying the ligand-N(CH3)(CD3) substrate provide further insights," wrote D. Maiti and colleagues, Johns Hopkins University.

The researchers concluded: "The mononuclear Cu-II(-OOH) entity or...

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