ArticleProceedings of the National Academy of Sciences of the United States of America2011
Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Conformational rigidity of cytochrome c'-α from a thermophile is associated with slow NO binding.Biophysical journal · 2024Article
- Computational infrared and Raman spectra by hybrid QM/MM techniques: a study on molecular and catalytic material systems.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2023Article
- A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-β: Implications for NO sensors.The Journal of biological chemistry · 2023Article
- A new paradigm for gaseous ligand selectivity of hemoproteins highlighted by soluble guanylate cyclase.Journal of inorganic biochemistry · 2021Review
- One fold, two functions: cytochrome P460 and cytochromeChemical science · 2019Article
- Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Distinguishing Nitro vs Nitrito Coordination in Cytochrome c' Using Vibrational Spectroscopy and Density Functional Theory.Inorganic chemistry · 2017Article
- Structural and functional analyses of pyroglutamate-amyloid-β-specific antibodies as a basis for Alzheimer immunotherapy.The Journal of biological chemistry · 2017Article
- Engineering proximalChemical science · 2017Article
- Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential.IUCrJ · 2015Review
- Conformational control of the binding of diatomic gases to cytochrome c'.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- NO* binds human cystathionine β-synthase quickly and tightly.The Journal of biological chemistry · 2014Article
- Modulation of ligand-heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond-second temporal range.The FEBS journal · 2013Article
- 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
- Discrimination between CO and O(2) in heme oxygenase: comparison of static structures and dynamic conformation changes following CO photolysis.Biochemistry · 2012Article
- Folding helical proteins in explicit solvent using dihedral-biased tempering.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A "sliding scale rule" for selectivity among NO, CO, and O₂ by heme protein sensors.Biochemistry · 2012Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Carbon monoxide (CO) is a product of haem metabolism and organisms must evolve strategies to prevent endogenous CO poisoning of haemoproteins. We show that energy costs associated with conformational changes play a key role in preventing irreversible CO binding. AxCYTcp is a member of a family of haem proteins that form stable 5c-NO and 6c-CO complexes but do not form O(2) complexes. Structure of the AxCYTcp-CO complex at 1.25 Å resolution shows that CO binds in two conformations moderated by the extent of displacement of the distal residue Leu16 toward the haem 7-propionate. The presence of two CO conformations is confirmed by cryogenic resonance Raman data. The preferred linear Fe-C-O arrangement (170 ± 8°) is accompanied by a flip of the propionate from the distal to proximal face of the haem. In the second conformation, the Fe-C-O unit is bent (158 ± 8°) with no flip of propionate. The energetic cost of the CO-induced Leu-propionate movements is reflected in a 600 mV (57.9 kJ mol(-1)) decrease in haem potential, a value in good agreement with density functional theory calculations. Substitution of Leu by Ala or Gly (structures determined at 1.03 and 1.04 Å resolutions) resulted in a haem site that binds CO in the linear mode only and where no significant change in redox potential is observed. Remarkably, these variants were isolated as ferrous 6c-CO complexes, attributable to the observed eight orders of magnitude increase in affinity for CO, including an approximately 10,000-fold decrease in the rate of dissociation. These new findings have wide implications for preventing CO poisoning of gas-binding haem proteins.
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