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Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism.

Abstract:

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...

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Publication status:
Published

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Publisher copy:
10.1021/ja2007017

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Journal:
Journal of the American Chemical Society
Volume:
133
Issue:
39
Pages:
15376-15383
Publication date:
2011-10-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:66723f50-9e3c-4f1b-b866-dcd3347aaf63
Source identifiers:
240699
Local pid:
pubs:240699

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