Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year

IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

See all formats and pricing
More options …
Volume 380, Issue 6 (Jun 1999)


Oxidation of 4-tert-Butylcatechol and Dopamine by Hydrogen Peroxide Catalysed by Horseradisch Peroxidase

M. García-Moreno / M. Moreno-Conesa / J.N. Rodríguez-López / F. García-Cánovas / R. Varón
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.1999.085


The catalytic cycle of horseradish peroxidase (HRP; donor:hydrogen peroxide oxidoreductase; EC is initiated by a rapid oxidation of it by hydrogen peroxide to give an enzyme intermediate, compound I, which reverts to the resting state via two successive single electron transfer reactions from reducing substrate molecules, the first yielding a second enzyme intermediate, compound II. To investigate the mechanism of action of horseradish peroxidase on catechol substrates we have studied the oxidation of both 4-tert-butylcatechol and dopamine catalysed by this enzyme. The different polarity of the side chains of both o-diphenol substrates could help in the understanding of the nature of the rate-limiting step in the oxidation of these substrates by the enzyme. The procedure used is based on the experimental data to the corresponding steady-state equations and permitted evaluation of the more significant individual rate constants involved in the corresponding reaction mechanism. The values obtained for the rate constants for each of the two substrates allow us to conclude that the reaction of horseradish peroxidase compound II with o-diphenols can be visualised as a two-step mechanism in which the first step corresponds to the formation of an enzyme-substrate complex, and the second to the electron transfer from the substrate to the iron atom. The size and hydrophobicity of the substrates control their access to the hydrophobic binding site of horseradish peroxidase, but electron density in the hydroxyl group of C-4 is the most important feature for the electron transfer step.

About the article

Published Online: 2005-06-01

Published in Print: 1999-06-01

Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.1999.085.

Export Citation

Copyright © 1999 by Walter de Gruyter GmbH & Co. KG. Copyright Clearance Center

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

D. A. Myasnikova, A. E. Polyakov, O. E. Vashkinskaya, S. V. Muginova, and T. N. Shekhovtsova
Moscow University Chemistry Bulletin, 2014, Volume 69, Number 2, Page 97
Francisco Rojas-Melgarejo, José Neptuno Rodrı́guez-López, Francisco Garcı́a-Cánovas, and Pedro Antonio Garcı́a-Ruiz
Process Biochemistry, 2004, Volume 39, Number 11, Page 1455
Thomas B. Brück and Patricia J. Harvey
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003, Volume 1649, Number 2, Page 154
L. I. Oleinik, T. S. Buslova, I. A. Veselova, and T. N. Shekhovtsova
Moscow University Chemistry Bulletin, 2011, Volume 66, Number 3, Page 166
María Angeles Gilabert, Lorena G. Fenoll, Francisco García-Molina, José Tudela, Francisco García-Cánovas, and José Neptuno Rodríguez-López
Biological Chemistry, 2004, Volume 385, Number 9
Lorraine C. Axford, Kate E. Holden, Katrin Hasse, Martin G. Banwell, Wolfgang Steglich, Jörg Wagler, and Anthony C. Willis
Australian Journal of Chemistry, 2008, Volume 61, Number 2, Page 80

Comments (0)

Please log in or register to comment.
Log in