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.
|Titolo:||Inhibitor binding studies on ascorbate oxidase|
BERINGHELLI, TIZIANA (Penultimo)
|Parole Chiave:||Ascorbate oxidase; Catalytic mechanism; Enzyme inhibition; Molecular mechanics; Spectroscopic studies|
|Settore Scientifico Disciplinare:||Settore CHIM/03 - Chimica Generale e Inorganica|
|Data di pubblicazione:||1999|
|Digital Object Identifier (DOI):||10.1016/S0010-8545(99)00014-4|
|Appare nelle tipologie:||01 - Articolo su periodico|