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Succinate:quinone oxidoreductases from epsilon-proteobacteria
C Roy D Lancaster1, Jörg Simon
1Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Frankfurt am Main, Germany. roy.lancaster@mpibp-frankfurt.mpg.de
Biochimica Et Biophysica Acta
|January 23, 2002
Summary
Epsilon-proteobacteria, including pathogenic species like Helicobacter, can respire using fumarate anaerobically. The succinate:quinone oxidoreductase enzyme complex is key to this process and a potential therapeutic target.
Area of Science:
- Microbiology
- Biochemistry
- Structural Biology
Background:
- Epsilon-proteobacteria are a diverse group, with many capable of anaerobic growth.
- Fumarate respiration is a common metabolic pathway in this bacterial subdivision.
- Pathogenic epsilon-proteobacteria pose significant health concerns.
Purpose of the Study:
- To investigate the role of succinate:quinone oxidoreductases in anaerobic fumarate respiration in epsilon-proteobacteria.
- To provide a structural model for these enzymes based on available genomic and crystallographic data.
- To highlight the potential of these enzymes as therapeutic targets.
Main Methods:
- Comparative genomic analysis of epsilon-proteobacteria.
- Biochemical assays for fumarate reduction.
- X-ray crystallography to determine enzyme structure.
- Bioinformatic analysis of enzyme complexes.
Main Results:
- Genes encoding succinate:quinone oxidoreductase (frdC, A, B) are conserved in epsilon-proteobacteria.
- Anaerobic fumarate respiration was confirmed in several epsilon-proteobacteria species.
- The crystal structure of the Wolinella succinogenes quinol:fumarate reductase complex (FrdCAB) was determined, providing a structural model.
- Succinate:quinone oxidoreductases are structurally similar across epsilon-proteobacteria.
Conclusions:
- Succinate:quinone oxidoreductases are crucial for anaerobic fumarate respiration in epsilon-proteobacteria.
- The structural insights into FrdCAB serve as a model for related enzymes.
- Targeting succinate:quinone oxidoreductases presents a promising strategy for developing therapeutics against pathogenic epsilon-proteobacteria.