Publications by authors named "Augusto Marchesini"
Article Synopsis
- Intramolecular electron transfer in zucchini squash ascorbate oxidase is inhibited by Ag(+) at equimolar concentrations, affecting the enzyme's activity.
- At pH 5.5, the enzyme is initially reduced at a high rate by a generated semiquinone, followed by a slower equilibration of the reducing equivalent to the trinuclear copper cluster.
- The presence of Ag(+) slows the return of the reducing equivalent to the Type I copper, leading to a decrease in the overall midpoint potential of the copper cluster and inhibiting enzyme activity.
The present investigation addresses the problem of the binding mode of phenolic inhibitors and the substrate ascorbate to the active site of ascorbate oxidase. The results from both types of compounds indicate that the binding site is located in a pocket near the type 1 copper center. This information is of general interest for blue multicopper oxidases.
View Article and Find Full Text PDF