ArticleBiophysical journal2019
A Thermodynamic Limit on the Role of Self-Propulsion in Enhanced Enzyme Diffusion.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Single molecule-driven nanomotors reveal the dynamic-disordered chemomechanical transduction of active enzymes.Science advances · 2025Article
- Mechanistic insights into condensate formation of human liver-type phosphofructokinase by stochastic modeling approaches.Scientific reports · 2024Article
- On the utility of microfluidic systems to study protein interactions: advantages, challenges, and applications.European biophysics journal : EBJ · 2023Review
- Response to Comment on "Following Molecular Mobility during Chemical Reactions: No Evidence for Active Propulsion" and "Molecular Diffusivity of Click Reaction Components: The Diffusion Enhancement Question".Journal of the American Chemical Society · 2022Article
- Enzyme Purification Improves the Enzyme Loading, Self-Propulsion, and Endurance Performance of Micromotors.ACS nano · 2022Article
- Perspective: a stirring role for metabolism in cells.Molecular systems biology · 2022Review
- Molecular Diffusivity of Click Reaction Components: The Diffusion Enhancement Question.Journal of the American Chemical Society · 2022Article
- Chemically-powered swimming and diffusion in the microscopic world.Nature reviews. Chemistry · 2021Review
- Single-molecule diffusometry reveals no catalysis-induced diffusion enhancement of alkaline phosphatase as proposed by FCS experiments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Enhanced Diffusion of Catalytically Active Enzymes.ACS central science · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A number of enzymes reportedly exhibit enhanced diffusion in the presence of their substrates, with a Michaelis-Menten-like concentration dependence. Although no definite explanation of this phenomenon has emerged, a physical picture of enzyme self-propulsion using energy from the catalyzed reaction has been widely considered. Here, we present a kinematic and thermodynamic analysis of enzyme self-propulsion that is independent of any specific propulsion mechanism. Using this theory, along with biophysical data compiled for all enzymes so far shown to undergo enhanced diffusion, we show that the propulsion speed required to generate experimental levels of enhanced diffusion exceeds the speeds of well-known active biomolecules, such as myosin, by several orders of magnitude. Furthermore, the minimal power dissipation required to account for enzyme enhanced diffusion by self-propulsion markedly exceeds the chemical power available from enzyme-catalyzed reactions. Alternative explanations for the observation of enhanced enzyme diffusion therefore merit stronger consideration.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.