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Updated: Aug 9, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis
Nicolas Rouhier1, Jean Pierre Jacquot
1UMR 1136 Interactions Arbres Microorganismes INRA UHP, Faculté des Sciences, P.O. Box 239, 54506 Vandoeuvre, France. nrouhier@scbiol.uhp-nancy.fr
Abstract:
A hybrid protein from Neisseria meningitidis, which contains both a peroxiredoxin and a glutaredoxin domain, has been isolated. The enzyme was active in the reduction of various peroxides and dehydroascorbate in the presence of reduced glutathione. These findings suggest that both the peroxiredoxin and glutaredoxin domains are biochemically active in the fusion. Moreover, when expressed separately, the glutaredoxin domain was catalytically active and the peroxiredoxin domain possessed a weak activity when supplemented with exogenous glutaredoxin.
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