ArticleProceedings of the National Academy of Sciences of the United States of America2018
Entropic contribution to enhanced thermal stability in the thermostable P450 CYP119.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 69 citations in OpenAlex.
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- Deep learning-guided dual-fitness evolution of T7 RNA polymerase for enhanced stability and activity.Nucleic acids research · 2026Article
- The Power of Protein Dynamics in Binding and Allostery.Biochemistry · 2026Review
- Characterisation of a Self-Sufficient Cytochrome P450 Enzyme From the Bacterium Thermosporothrix hazakensis and Its Conversion Into a Peroxygenase.Microbial biotechnology · 2025Article
- Function and Engineering of a Food Enzyme Under Coupled High-Temperature-Pressure Conditions: Insights from Molecular Dynamics Simulation and Experimental Validation.Foods (Basel, Switzerland) · 2025Article
- Insights into the low-temperature adaptation of an enzyme as studied through ancestral sequence reconstruction.Protein science : a publication of the Protein Society · 2025Article
- Optimizing enzyme thermostability by combining multiple mutations using protein language model.mLife · 2024Article
- Temperature-dependent iron motion in extremophile rubredoxins - no need for 'corresponding states'.Scientific reports · 2024Article
- Characterization of the pH-dependent protein stability of 3α-hydroxysteroid dehydrogenase/carbonyl reductase by differential scanning fluorimetry.Protein science : a publication of the Protein Society · 2023Article
- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- Thermostability engineering of industrial enzymes through structure modification.Applied microbiology and biotechnology · 2022Review
- Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity.Nucleic acids research · 2022Article
- Engineering Strategies to Overcome the Stability-Function Trade-Off in Proteins.ACS synthetic biology · 2022Review
- Controlling the Substrate Specificity of an Enzyme through Structural Flexibility by Varying the Salt-Bridge Density.Molecules (Basel, Switzerland) · 2021Article
- Locking out water at 100°C.Biophysical journal · 2021Article
- Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.Biophysical journal · 2021Article
- An experimental approach probing the conformational transitions and energy landscape of antibodies: a glimmer of hope for reviving lost therapeutic candidates using ionic liquid.Chemical science · 2021Article
- A dynamic understanding of cytochrome P450 structure and function through solution NMR.Current opinion in biotechnology · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enhanced thermostability of thermophilic proteins with respect to their mesophilic counterparts is often attributed to the enthalpy effect, arising from strong interactions between protein residues. Intuitively, these strong interresidue interactions will rigidify the biomolecules. However, the present work utilizing neutron scattering and solution NMR spectroscopy measurements demonstrates a contrary example that the thermophilic cytochrome P450, CYP119, is much more flexible than its mesophilic counterpart, CYP101A1, something which is not apparent just from structural comparison of the two proteins. A mechanism to explain this apparent contradiction is that higher flexibility in the folded state of CYP119 increases its conformational entropy and thereby reduces the entropy gain during denaturation, which will increase the free energy needed for unfolding and thus stabilize the protein. This scenario is supported by thermodynamic data on the temperature dependence of unfolding free energy, which shows a significant entropic contribution to the thermostability of CYP119 and lends an added dimension to enhanced stability, previously attributed only to presence of aromatic stacking interactions and salt bridge networks. Our experimental data also support the notion that highly thermophilic P450s such as CYP119 may use a mechanism that partitions flexibility differently from mesophilic P450s between ligand binding and thermal stability.
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