The oxidized (3,3) state of manganese catalase. Comparison of enzymes from Thermus thermophilus and Lactobacillus plantarum

Mei M. Whittaker, Vladimir V. Barynin, Svetlana V. Antonyuk, James Whittaker

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

Manganese catalases contain a binuclear manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting between dimanganese(II) [(2,2)] and dimanganese(III) [(3,3)] oxidation states during turnover. We have investigated the oxidized (3,3) states of the homologous enzymes from Thermus thermophilus and Lactobacillus plantarum using a combination of optical absorption, CD, MCD, and EPR spectroscopies as sensitive probes of the electronic structure and protein environment for the active site metal clusters. Comparison of results for these two enzymes allows the essential features of the active sites to be recognized and the differences identified. For both enzymes, preparations having the highest catalytic activity have diamagnetic ground states, consistent with the bis- μ-bridging dimanganese core structure that has been defined crystallographically. Oxidative damage and exogenous ligand binding perturb the core structure of LPC, converting the enzyme to a distinct form in which the cluster becomes paramagnetic as a result of altered exchange coupling mediated by the bridging ligands. The TTC cluster does not exhibit this sensitivity to ligand binding, implying a different reactivity for the bridges in that enzyme. A mechanism is proposed involving distinct coordination modes for peroxide substrate in each of the two half-reactions for enzyme turnover.

Original languageEnglish (US)
Pages (from-to)9126-9136
Number of pages11
JournalBiochemistry
Volume38
Issue number28
DOIs
StatePublished - Jul 13 1999

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Thermus thermophilus
Lactobacillus plantarum
Catalase
Enzymes
Ligands
Catalytic Domain
Exchange coupling
Peroxides
Manganese
Light absorption
Ground state
Hydrogen Peroxide
Oxidation-Reduction
Electronic structure
Paramagnetic resonance
Catalyst activity
Spectrum Analysis
Metals
Spectroscopy
Oxidation

ASJC Scopus subject areas

  • Biochemistry

Cite this

The oxidized (3,3) state of manganese catalase. Comparison of enzymes from Thermus thermophilus and Lactobacillus plantarum. / Whittaker, Mei M.; Barynin, Vladimir V.; Antonyuk, Svetlana V.; Whittaker, James.

In: Biochemistry, Vol. 38, No. 28, 13.07.1999, p. 9126-9136.

Research output: Contribution to journalArticle

Whittaker, Mei M. ; Barynin, Vladimir V. ; Antonyuk, Svetlana V. ; Whittaker, James. / The oxidized (3,3) state of manganese catalase. Comparison of enzymes from Thermus thermophilus and Lactobacillus plantarum. In: Biochemistry. 1999 ; Vol. 38, No. 28. pp. 9126-9136.
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