The characteristic features of the plant multicopper enzyme ascorbate oxidase are described, together with the current knowledge about its catalytic mechanism and substrate specificity. A variety of small anionic inhibitors have been used as spectroscopic probes for the enzyme metal sites, but recently interest has arisen for a new type of phenolic inhibitors which act competitively against ascorbate. These simple phenolic compounds can bind to the enzyme in the same pocket near type 1 copper as the substrate ascorbate binds, as shown by docking and molecular mechanics computations. (C) 1999 Elsevier Science S.A. All rights reserved.

Inhibitor binding studies on ascorbate oxidase / L. Casella, E. Monzani, L. Santagostini, L. Gioia, M. Gullotti, P. Fantucci, T. Beringhelli, A. Marchesini. - In: COORDINATION CHEMISTRY REVIEWS. - ISSN 0010-8545. - 185-6(1999), pp. 619-628.

Inhibitor binding studies on ascorbate oxidase

L. Santagostini;T. Beringhelli
Penultimo
;
1999

Abstract

The characteristic features of the plant multicopper enzyme ascorbate oxidase are described, together with the current knowledge about its catalytic mechanism and substrate specificity. A variety of small anionic inhibitors have been used as spectroscopic probes for the enzyme metal sites, but recently interest has arisen for a new type of phenolic inhibitors which act competitively against ascorbate. These simple phenolic compounds can bind to the enzyme in the same pocket near type 1 copper as the substrate ascorbate binds, as shown by docking and molecular mechanics computations. (C) 1999 Elsevier Science S.A. All rights reserved.
Ascorbate oxidase; Catalytic mechanism; Enzyme inhibition; Molecular mechanics; Spectroscopic studies
Settore CHIM/03 - Chimica Generale e Inorganica
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/188904
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