Quinone- and nitroreductase reactions of Thermotoga maritima thioredoxin reductase

• Authors: Benjaminas Valiauga , Nicolas Rouhier , Jean-Pierre Jacquot , Narimantas Čėnas
• Languages of publication: EN

Abstracts

EN

The Thermotoga maritima NADH:thioredoxin reductase (TmTR) contains FAD and a catalytic disulfide in the active center, and uses a relatively poorly studied physiological oxidant Grx-1-type glutaredoxin. In order to further assess the redox properties of TmTR, we used series of quinoidal and nitroaromatic oxidants with a wide range of single-electron reduction potentials (E17, -0.49-0.09 V). We found that TmTR catalyzed the mixed single- and two-electron reduction of quinones and nitroaromatic compounds, which was much faster than the reduction of Grx-1. The reactivity of both groups of oxidants increased with an increase in their E17, thus pointing to the absence of their structural specificity. The maximal rates of quinone reduction in the steady-state reactions were lower than the maximal rates of reduction of FAD by NADH, obtained in presteady-state experiments. The mixed-type reaction inhibition by NAD+ was consistent with its competition for a NADH binding site in the oxidized enzyme form, and also with the reoxidation of the reduced enzyme form. The inhibition data yielded a value of the standard potential for TmTR of -0.31±0.03 V at pH 7.0, which may correspond to the FAD/FADH2 redox couple. Overall, the mechanism of quinone- and nitroreductase reactions of T. maritima TR was similar to the previously described mechanism of Arabidopsis thaliana TR, and points to their prooxidant and possibly cytotoxic role.

Keywords

EN

thioredoxin reductase; quinones; nitroaromatic compounds; oxidative stress; Thermotoga

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2015
• Volume: 62
• Issue: 2
• Pages: 303-309

Dates

published

2015

received

2015-03-06

revised

2015-04-08

accepted

2015-04-28

(unknown)

2015-06-22

Contributors

author

Benjaminas Valiauga

• Institute of Biochemistry of Vilnius University, LT-08662 Vilnius, Lithuania

author

Nicolas Rouhier

• Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France
• INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux, France

author

Jean-Pierre Jacquot

• Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France
• INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux, France

author

Narimantas Čėnas

• Institute of Biochemistry of Vilnius University, LT-08662 Vilnius, Lithuania

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Identifiers

DOI

10.18388/abp.2015_1003