Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism.
We test the hypothesized pathway by which protons are passed from the substrate, ascorbate, to the ferryl oxygen in the heme enzyme ascorbate peroxidase (APX). The role of amino acid side chains and bound solvent is demonstrated. We investigated solvent kinetic isotope effects (SKIE) for the wild-type enzyme and several site-directed replacements of the key residues which form the proposed proton path. Kinetic constants for H(2)O(2)-dependent enzyme oxidation to Compound I, k(1), and subseque...Expand abstract
- Publication status:
- Publisher copy:
- Copyright date:
Views and Downloads
If you are the owner of this record, you can report an update to it here: Report update to this record