Respiratory inhibitors activate an Fnr-like regulatory protein in Paracoccus denitrificans: implications for the regulation of the denitrification pathway
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
8019429
Knihovny.cz E-resources
- MeSH
- Aerobiosis MeSH
- Anaerobiosis MeSH
- Azides pharmacology MeSH
- Bacterial Proteins metabolism MeSH
- beta-Galactosidase biosynthesis metabolism MeSH
- Nitrogen metabolism MeSH
- Cyanides pharmacology MeSH
- Nitrate Reductases biosynthesis metabolism MeSH
- Nitrite Reductases biosynthesis metabolism MeSH
- Nitrogen Dioxide pharmacology MeSH
- Oxidation-Reduction MeSH
- Oxygenases antagonists & inhibitors metabolism MeSH
- Paracoccus denitrificans chemistry drug effects physiology MeSH
- Iron-Sulfur Proteins * MeSH
- Escherichia coli Proteins * MeSH
- Rotenone pharmacology MeSH
- Oxygen Consumption drug effects MeSH
- Electron Transport drug effects MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Azides MeSH
- Bacterial Proteins MeSH
- beta-Galactosidase MeSH
- Nitrogen MeSH
- FNR protein, E coli MeSH Browser
- Cyanides MeSH
- Nitrate Reductases MeSH
- Nitrite Reductases MeSH
- Nitrogen Dioxide MeSH
- Oxygenases MeSH
- Iron-Sulfur Proteins * MeSH
- Escherichia coli Proteins * MeSH
- Rotenone MeSH
Unlike the uncoupler carbonyl cyanide 3-chlorophenyl-hydrazone, the respiratory inhibitors CN-, N3-, NO2- and rotenone enhanced the formation of nitrate and nitrite reductases in highly aerated cultures of the Paracoccus denitrificans ex-conjugant PD1222 (pRW2A/FF). A maximal effect was observed at concentrations partly blocking electron transport to O2. The level of beta-galactosidase reporting the activity of an Fnr-like regulatory protein showed a similar concentration dependency. It is concluded that oxygen is sensed by Fnr in an indirect way, possibly via the redox state of a cellular component.
Control of gene expression by FNR-like proteins in facultatively anaerobic bacteria
