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Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Structure and function of YcnD from Bacillus subtilis, a flavin-containing oxidoreductase
Alexander Morokutti1, Andrzej Lyskowski, Sonja Sollner
1Institut für Biochemie, Technische Universität Graz, A-8010 Graz, Austria.
Biochemistry
|October 19, 2005
Summary
Bacillus subtilis YcnD is an FMN-containing oxidoreductase. This enzyme utilizes NADPH as its physiological reductant and can reduce nitro-organic compounds, chromate, and azo dyes, suggesting a role in delivering reduced FMN.
Area of Science:
- Biochemistry
- Structural Biology
- Microbiology
Background:
- YcnD is a protein from Bacillus subtilis belonging to the oxidoreductase family.
- These enzymes are known to utilize NADH and/or NADPH.
Purpose of the Study:
- To biochemically characterize purified YcnD.
- To determine the enzyme's structure and elucidate its physiological function.
Main Methods:
- Protein purification and biochemical assays (enzyme kinetics, substrate reduction).
- X-ray crystallography for structure determination.
Main Results:
- YcnD is an FMN-containing enzyme reduced by NADH and NADPH, with NADPH being the likely physiological reductant.
- The enzyme reduces nitro-organic compounds, chromate, and azo dyes, with azo dye reduction dependent on free reduced FMN.
- X-ray crystallography revealed YcnD folds into an alpha-beta-alpha sandwich and forms homodimers, similar to the NADH oxidase superfamily.
Conclusions:
- YcnD functions as an oxidoreductase, likely delivering reduced FMN to other enzymes.
- The structural and biochemical data provide insights into YcnD's role in Bacillus subtilis.
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