ArticleProceedings of the National Academy of Sciences of the United States of America2009
The O2 sensitivity of the transcription factor FNR is controlled by Ser24 modulating the kinetics of [4Fe-4S] to [2Fe-2S] conversion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Escherichia coli growing under antimicrobial gallium nitrate stress reveals new processes of tolerance and toxicity.Scientific reports · 2025Article
- WhiB-like proteins: Diversity of structure, function and mechanism.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Oxygen is an essential gasotransmitter directly sensed via protein gasoreceptors.Animal models and experimental medicine · 2024Article
- A multi-scale expression and regulation knowledge base for Escherichia coli.Nucleic acids research · 2023Article
- The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress.Journal of the American Chemical Society · 2022Article
- The PhoPR two-component system responds to oxygen deficiency and regulates the pathways for energy supply in Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2021Article
- Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Article
- Identification and Unusual Properties of the Master Regulator FNR in the Extreme AcidophileFrontiers in microbiology · 2019Article
- Reassessing the Structure and Function Relationship of the OAntioxidants & redox signaling · 2018Review
- Development of heme protein based oxygen sensing indicators.Scientific reports · 2018Article
- Hierarchical interactions between Fnr orthologs allows fine-tuning of transcription in response to oxygen in Herbaspirillum seropedicae.Nucleic acids research · 2018Article
- Biochemical characterization and essentiality ofThe Journal of biological chemistry · 2018Article
- Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization.Protein expression and purification · 2017Article
- Strategies for manipulation of oxygen utilization by the electron transfer chain in microbes for metabolic engineering purposes.Journal of industrial microbiology & biotechnology · 2017Review
- Mass spectrometric identification of intermediates in the OProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Rapid Sampling of Escherichia coli After Changing Oxygen Conditions Reveals Transcriptional Dynamics.Genes · 2017Article
- Alkene hydrogenation activity of enoate reductases for an environmentally benign biosynthesis of adipic acid.Chemical science · 2017Article
- Discrimination and Integration of Stress Signals by Pathogenic Bacteria.Cell host & microbe · 2016Review
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8 authors.
Funding
Abstract
Fumarate and nitrate reduction regulatory (FNR) proteins are bacterial transcription factors that coordinate the switch between aerobic and anaerobic metabolism. In the absence of O(2), FNR binds a [4Fe-4S](2+) cluster (ligated by Cys-20, 23, 29, 122) promoting the formation of a transcriptionally active dimer. In the presence of O(2), FNR is converted into a monomeric, non-DNA-binding form containing a [2Fe-2S](2+) cluster. The reaction of the [4Fe-4S](2+) cluster with O(2) has been shown to proceed via a 2-step process, an O(2)-dependent 1-electron oxidation to yield a [3Fe-4S](+) intermediate with release of 1 Fe(2+) ion, followed by spontaneous rearrangement to the [2Fe-2S](2+) form with release of 1 Fe(3+) and 2 S(2-) ions. Here, we show that replacement of Ser-24 by Arg, His, Phe, Trp, or Tyr enhances aerobic activity of FNR in vivo. The FNR-S24F protein incorporates a [4Fe-4S](2+) cluster with spectroscopic properties similar to those of FNR. However, the substitution enhances the stability of the [4Fe-4S](2+) cluster in the presence of O(2). Kinetic analysis shows that both steps 1 and 2 are slower for FNR-S24F than for FNR. A molecular model suggests that step 1 of the FNR-S24F iron-sulfur cluster reaction with O(2) is inhibited by shielding of the iron ligand Cys-23, suggesting that Cys-23 or the cluster iron bound to it is a primary site of O(2) interaction. These data lead to a simple model of the FNR switch with physiological implications for the ability of FNR proteins to operate over different ranges of in vivo O(2) concentrations.
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