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Flavodoxin from Wolinella succinogenes
1Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germany.
Archives of Microbiology
|August 1, 1996
Summary
Flavodoxin, a protein in Wolinella succinogenes, primarily supports anabolic processes, not energy-producing catabolic functions. This flavodoxin plays a key role in cellular biosynthesis.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Wolinella succinogenes utilizes fumarate or polysulfide as terminal electron acceptors.
- Flavodoxins are electron transfer proteins crucial in various metabolic pathways.
Purpose of the Study:
- To isolate and characterize flavodoxin from Wolinella succinogenes.
- To determine the function of flavodoxin in W. succinogenes metabolism, distinguishing between anabolic and catabolic roles.
Main Methods:
- Isolation and purification of a monomeric flavoprotein (18.8 kDa).
- N-terminal sequencing, FMN content analysis, and redox potential measurements.
- Enzyme activity assays for pyruvate:flavodoxin oxidoreductase and electron transfer from donor enzymes.
Main Results:
- Isolated flavoprotein identified as flavodoxin (Fld) with specific redox potentials (-95 mV and -450 mV at pH 7.5).
- Flavodoxin content remained consistent irrespective of growth conditions (fumarate or polysulfide).
- Flavodoxin did not interact with known electron donor enzymes (hydrogenase, formate dehydrogenase) but showed activity with pyruvate:flavodoxin oxidoreductase.
Conclusions:
- Flavodoxin in W. succinogenes is not involved in electron transport to terminal acceptors.
- The enzyme pyruvate:flavodoxin oxidoreductase utilizes flavodoxin, suggesting a role in biosynthesis.
- Flavodoxin likely serves anabolic functions in W. succinogenes rather than catabolic ones.