Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase

Olaniyi Opaleye, Ruth Sarah Rose, Mei M. Whittaker, Eui Jeon Woo, James Whittaker, Richard W. Pickersgill

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Abstract

Oxalate oxidase (EC 1.2.3.4) catalyzes the conversion of oxalate and dioxygen to hydrogen peroxide and carbon dioxide. In this study, glycolate was used as a structural analogue of oxalate to investigate substrate binding in the crystalline enzyme. The observed monodentate binding of glycolate to the active site manganese ion of oxalate oxidase is consistent with a mechanism involving C-C bond cleavage driven by superoxide anion attack on a monodentate coordinated substrate. In this mechanism, the metal serves two functions: to organize the substrates (oxalate and dioxygen) and to transiently reduce dioxygen. The observed structure further implies important roles for specific active site residues (two asparagines and one glutamine) in correctly orientating the substrates and reaction intermediates for catalysis. Combined spectroscopic, biochemical, and structural analyses of mutants confirms the importance of the asparagine residues in organizing a functional active site complex.

Original languageEnglish (US)
Pages (from-to)6428-6433
Number of pages6
JournalJournal of Biological Chemistry
Volume281
Issue number10
DOIs
Publication statusPublished - Mar 10 2006

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Opaleye, O., Rose, R. S., Whittaker, M. M., Woo, E. J., Whittaker, J., & Pickersgill, R. W. (2006). Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase. Journal of Biological Chemistry, 281(10), 6428-6433. https://doi.org/10.1074/jbc.M510256200