Elucidation of the factors affecting the oxidative activity of Acremonium sp. HI-25 ascorbate oxidase by an electrochemical approach.
Steady-state kinetics of Acremonium sp. HI-25 ascorbate oxidase toward p-hydroquinone derivatives have been examined by using an electrochemical analysis based on the theory of steady-state bioelectrocatalysis. The electrochemical technique has enabled one to examine the influence of electronic and chemical properties of substrates on the activity. It was proven that the oxidative activity of ascorbate oxidase was dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between ascorbate oxidase's type 1 copper site and substrate.
Murata
Kenichi
K
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, Japan.
Nakamura
Nobuhumi
N
Ohno
Hiroyuki
H
D000164:Acremonium / Q000201:enzymology*; D001204:Ascorbate Oxidase / Q000737:chemistry*; D002384:Catalysis; D003198:Computer Simulation; D003300:Copper / Q000737:chemistry*; D004563:Electrochemistry / Q000379:methods*; D004789:Enzyme Activation; D004795:Enzyme Stability; D007700:Kinetics; D008956:Models, Chemical; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D003300:Copper; D001204:Ascorbate Oxidase