ArticleBiophysical journal2005
Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Review
- Automated Flow Synthesis of Artificial Heme Enzymes for Enantiodivergent Biocatalysis.Journal of the American Chemical Society · 2025Article
- Heme pocket modulates protein conformation and diguanylate cyclase activity of a tetrameric globin coupled sensor.Journal of inorganic biochemistry · 2024Article
- Oxygen-selective regulation of cyclic di-GMP synthesis by a globin coupled sensor with a shortened linking domain modulates Shewanella sp. ANA-3 biofilm.Journal of inorganic biochemistry · 2024Article
- Noncanonical Sensing Mechanisms for Bacillus subtilis Chemoreceptors.Journal of bacteriology · 2022Article
- Characterization of Opposing Responses to Phenol by Bacillus subtilis Chemoreceptors.Journal of bacteriology · 2022Article
- Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Hydrogen Sulfide and Carbon Monoxide Tolerance in Bacteria.Antioxidants (Basel, Switzerland) · 2021Review
- The Unconventional Cytoplasmic Sensing Mechanism for Ethanol Chemotaxis in Bacillus subtilis.mBio · 2020Article
- Protein Dynamics of the Sensor Protein HemAT as Probed by Time-Resolved Step-Scan FTIR Spectroscopy.Biophysical journal · 2018Article
- Coordination and redox state-dependent structural changes of the heme-based oxygen sensorThe Journal of biological chemistry · 2017Article
- Mechanism and Role of Globin-Coupled Sensor Signalling.Advances in microbial physiology · 2017Review
- Logarithmic sensing inNPJ systems biology and applications · 2017Article
- An O2-sensing stressosome from a Gram-negative bacterium.Nature communications · 2016Article
- Physical limits on bacterial navigation in dynamic environments.Journal of the Royal Society, Interface · 2016Article
- Taxis toward hydrogen gas by Methanococcus maripaludis.Scientific reports · 2013Article
- Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis.The Journal of biological chemistry · 2013Review
- Studies of bacterial aerotaxis in a microfluidic device.Lab on a chip · 2012Article
- How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase.Antioxidants & redox signaling · 2012Review
- Site-specific protein dynamics in communication pathway from sensor to signaling domain of oxygen sensor protein, HemAT-Bs: Time-resolved Ultraviolet Resonance Raman Study.The Journal of biological chemistry · 2012Article
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3 authors.
Funding
Abstract
HemAT from Bacillus subtilis is a new type of heme protein responsible for sensing oxygen. The structural and functional properties of the full-length HemAT protein, the sensor domain (1-178), and Tyr-70 mutants have been characterized. Kinetic and equilibrium measurements reveal that both full-length HemAT and the sensor domain show two distinct O(2) binding components. The high-affinity component has a K(dissociation) approximately 1-2 microM and a normal O(2) dissociation rate constant, k(O2) = 50-80 s(-1). The low-affinity component has a K(dissociation) approximately 50-100 microM and a large O(2) dissociation rate constant equal to approximately 2000 s(-1). The low n-value and biphasic character of the equilibrium curve indicate that O(2) binding to HemAT involves either independent binding to high- and low-affinity subunits in the dimer or negative cooperativity. Replacement of Tyr-70(B10) with Phe, Leu, or Trp in the sensor domain causes dramatic increases in k(O2) for both the high- and low-affinity components. In contrast, the rates and affinity for CO binding are little affected by loss of the Tyr-70 hydroxyl group. These results suggest highly dynamic behavior for the Tyr-70 side chain and the fraction of the "up" versus "down" conformation is strongly influenced by the nature of the iron-ligand complex. As a result of having both high- and low-affinity components, HemAT can respond to oxygen concentration gradients under both hypoxic (0-10 microM) and aerobic (50-250 microM) conditions, a property which could, in principle, be important for a robust sensing system. The unusual ligand-binding properties of HemAT suggest that asymmetry and apparent negative cooperativity play an important role in the signal transduction pathway.
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