Dumarieh, Rania and D'Antonio, Jennifer and Deliz-Liang, Alexandria and Smirnova, Tatyana and Svistunenko, Dimitri A and Ghiladi, Reza A (2013) Tyrosyl Radicals in Dehaloperoxidase. Journal of Biological Chemistry, 288 (46). pp. 33470-33482. DOI https://doi.org/10.1074/jbc.m113.496497
Dumarieh, Rania and D'Antonio, Jennifer and Deliz-Liang, Alexandria and Smirnova, Tatyana and Svistunenko, Dimitri A and Ghiladi, Reza A (2013) Tyrosyl Radicals in Dehaloperoxidase. Journal of Biological Chemistry, 288 (46). pp. 33470-33482. DOI https://doi.org/10.1074/jbc.m113.496497
Dumarieh, Rania and D'Antonio, Jennifer and Deliz-Liang, Alexandria and Smirnova, Tatyana and Svistunenko, Dimitri A and Ghiladi, Reza A (2013) Tyrosyl Radicals in Dehaloperoxidase. Journal of Biological Chemistry, 288 (46). pp. 33470-33482. DOI https://doi.org/10.1074/jbc.m113.496497
Abstract
Dehaloperoxidase (DHP) from Amphitrite ornata, having been shown to catalyze the hydrogen peroxide-dependent oxidation of trihalophenols to dihaloquinones, is the first oxygen binding globin that possesses a biologically relevant peroxidase activity. The catalytically competent species in DHP appears to be Compound ES, a reactive intermediate that contains both a ferryl heme and a tyrosyl radical. By simulating the EPR spectra of DHP activated by H2O2, Thompson et al. (Thompson, M. K., Franzen, S., Ghiladi, R. A., Reeder, B. J., and Svistunenko, D. A. (2010) J. Am. Chem. Soc. 132, 17501-17510) proposed that two different radicals, depending on the pH, are formed, one located on either Tyr-34 or Tyr-28 and the other on Tyr-38. To provide additional support for these simulation-based assignments and to deduce the role(s) that tyrosyl radicals play in DHP, stoppedflow UV-visible and rapid-freeze-quench EPR spectroscopic methods were employed to study radical formation in DHP when three tyrosine residues, Tyr-28, Tyr-34, and Tyr-38, were replaced either individually or in combination with phenylalanines. The results indicate that radicals form on all three tyrosines in DHP. Evidence for the formation of DHP Compound I in several tyrosine mutants was obtained. Variants that formed Compound I showed an increase in the catalytic rate for substrate oxidation but also an increase in heme bleaching, suggesting that the tyrosines are necessary for protecting the enzyme from oxidizing itself. This protective role of tyrosines is likely an evolutionary adaptation allowing DHP to avoid selfinflicted damage in the oxidative environment. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
Item Type: | Article |
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Uncontrolled Keywords: | Hemoglobin; Iron; Peroxidase; Radicals; Tyrosine; Compound ES; Compound I; Compound II; Dehaloperoxidase; Ferryl |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 09 Jan 2015 11:02 |
Last Modified: | 30 Oct 2024 20:12 |
URI: | http://repository.essex.ac.uk/id/eprint/10466 |