ArticleProceedings of the National Academy of Sciences of the United States of America2018
Slow domain reconfiguration causes power-law kinetics in a two-state enzyme.
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 13 papers.
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13 citing papers in PubMed.
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- Model-free photon analysis of diffusion-based single-molecule FRET experiments.Nature communications · 2025Article
- High-order Michaelis-Menten equations allow inference of hidden kinetic parameters in enzyme catalysis.Nature communications · 2025Article
- Perspective: How Fast Dynamics Affect Slow Function in Protein Machines.The journal of physical chemistry. B · 2023Review
- Dynamic Heterogeneity in the Optical Signals from Single Nano-Objects.The journal of physical chemistry. B · 2023Review
- Interplay of Polarity and Confinement in Asymmetric Catalysis with Chiral Rh Diene Complexes in Microemulsions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Single-molecule conformational dynamics of a transcription factor reveals a continuum of binding modes controlling association and dissociation.Nucleic acids research · 2021Article
- Diffusion of a disordered protein on its folded ligand.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Factors underlying asymmetric pore dynamics of disaggregase and microtubule-severing AAA+ machines.Biophysical journal · 2021Article
- Membrane Chemistry Tunes the Structure of a Peptide Transporter.Angewandte Chemie (International ed. in English) · 2020Article
- Single-Molecule Test for Markovianity of the Dynamics along a Reaction Coordinate.The journal of physical chemistry letters · 2018Article
- Transient antibody-antigen interactions mediate the strain-specific recognition of a conserved malaria epitope.Communications biology · 2018Article
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4 authors.
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Abstract
Protein dynamics are typically captured well by rate equations that predict exponential decays for two-state reactions. Here, we describe a remarkable exception. The electron-transfer enzyme quiescin sulfhydryl oxidase (QSOX), a natural fusion of two functionally distinct domains, switches between open- and closed-domain arrangements with apparent power-law kinetics. Using single-molecule FRET experiments on time scales from nanoseconds to milliseconds, we show that the unusual open-close kinetics results from slow sampling of an ensemble of disordered domain orientations. While substrate accelerates the kinetics, thus suggesting a substrate-induced switch to an alternative free energy landscape of the enzyme, the power-law behavior is also preserved upon electron load. Our results show that the slow sampling of open conformers is caused by a variety of interdomain interactions that imply a rugged free energy landscape, thus providing a generic mechanism for dynamic disorder in multidomain enzymes.
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