Inhibitor binding studies on ascorbate oxidase

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.