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Periplasmic methacrylate reductase activity in Wolinella succinogenes
1Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität, Marie-Curie-Strasse 9, 60439 Frankfurt am Main, Germany.
Archives of Microbiology
|October 31, 2001
Summary
Wolinella succinogenes utilizes methacrylate and acrylate for oxidation, with the fccABC operon playing a key role. Researchers identified potential enzymes involved in these crucial metabolic processes.
Area of Science:
- Microbiology
- Biochemistry
- Enzymology
Background:
- Wolinella succinogenes is a bacterium known for its unique metabolic pathways.
- The fccABC operon's role in W. succinogenes metabolism was previously unclear.
Purpose of the Study:
- To investigate the role of the fccABC operon in W. succinogenes.
- To identify the enzymes responsible for methacrylate and acrylate reduction.
Main Methods:
- Enzyme assays using cell homogenates and soluble fractions.
- Analysis of mutants lacking specific genes within the fccABC operon.
- Enzyme kinetics studies to determine kinetic parameters (Km and Vmax).
Main Results:
- W. succinogenes catalyzed the oxidation of benzyl viologen radical by methacrylate and acrylate.
- A mutant lacking the fccABC operon showed no activity for methacrylate or acrylate reduction.
- The periplasmic flavoprotein FccA, potentially in complex with FccB, is suggested to catalyze these reactions.
Conclusions:
- The fccABC operon is essential for methacrylate and acrylate reduction in W. succinogenes.
- FccA, possibly with FccB, is likely responsible for these catalytic activities.
- The overall metabolic function of the fccABC operon remains to be elucidated.