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Relationship between structure and function of the NADH oxidase from Lactobacillus brevis
Mathieu Dondelinger1, Marylène S Vandevenne1, Frédéric Kerff1
1Centre d'Ingénierie des Protéines, InBios, University of Liege, 13 Allée du 6 Août, B-4000, Liège, Belgium.
Biochimie
|January 19, 2026
Summary
NADH oxidases, crucial for bacterial defense and industrial use, require FAD cofactor. This study details the pH-dependent activation of Lactobacillus brevis NADH oxidase (LbNOX), revealing FAD
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Water-producing NADH oxidases are FAD-dependent enzymes vital for bacterial oxidative stress defense.
- Their NAD+ recycling capability makes them attractive for industrial oxidoreductive processes.
- Recombinant production often yields apoenzymes requiring FAD activation.
Purpose of the Study:
- To characterize the NADH oxidase from Lactobacillus brevis (LbNOX), a homodimeric flavoenzyme.
- To elucidate the pH-dependent activation mechanism and structural basis of LbNOX.
- To guide the development of robust protocols for producing active and homogeneous LbNOX.
Main Methods:
- Purification and formulation of LbNOX.
- Analysis of enzyme activity and oligomeric state dependence on pH and FAD.
- Comprehensive bioinformatic and structural analysis of LbNOX.
Main Results:
- LbNOX production and purification yielded a heterogeneous enzyme solution.
- The active dimeric form of LbNOX is pH-dependent and requires FAD.
- Bioinformatic analysis identified key residues for pH-dependent dimerization, with FAD bound at the dimer interface.
Conclusions:
- The structural and functional characterization of LbNOX is essential for understanding its FAD-dependent activation.
- This study provides insights for developing reproducible protocols for active LbNOX production.
- Findings support the advancement of NADH oxidases in industrial applications.
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