Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 290, Issue 3, Pages 1689-1698Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.618629
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Funding
- French State Grants [ANR-10-LABX-0040-SPS, ANR-11-IDEX-0003-02]
- ANR [JC 12-0001-01]
- CNRS
- Universite Paris Sud
- French Ministry of Higher Education and Research
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In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase enzyme chemistry from C-3 and C-4 plant species, we analyzed kinetic parameters of purified recombinant C-3 (Arabidopsis thaliana) and C-4 (Zea mays) plant enzymes and compared isotope effects using natural and deuterated glycolate in either natural or deuterated solvent. The C-12/C-13 isotope effect was also investigated for each plant glycolate oxidase protein by measuring the C-13 natural abundance in glycolate using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an hydrogen/deuterium isotope effect and that glycolate alpha-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C-3 and C-4 enzymes.
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