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Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
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C. elegans Chemotaxis Assay
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Enzyme leaps fuel antichemotaxis.

Ah-Young Jee1, Sandipan Dutta1, Yoon-Kyoung Cho1,2

  • 1Center for Soft and Living Matter, Institute for Basic Science, Ulsan 44919, South Korea.

Proceedings of the National Academy of Sciences of the United States of America
|December 20, 2017
PubMed
Summary
This summary is machine-generated.

Active enzymes exhibit enhanced diffusivity and move towards lower substrate concentrations, a process termed antichemotaxis. This enzyme behavior, observed via superresolution microscopy, mimics microbial foraging strategies.

Keywords:
FCSactive matterchemotaxisenzymefluorescence correlation spectroscopy

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Area of Science:

  • Biophysics
  • Chemical Kinetics
  • Enzymology

Background:

  • Enzyme catalytic activity is increasingly linked to altered physical properties, such as diffusivity.
  • Understanding enzyme movement is crucial for comprehending cellular processes and designing artificial systems.

Purpose of the Study:

  • To investigate the movement patterns of catalytically active enzymes.
  • To elucidate the mechanism behind enzyme migration in response to substrate gradients.
  • To explore the potential applications of enzyme-driven movement in synthetic systems.

Main Methods:

  • Utilized superresolution microscopy, specifically stimulated emission-depletion fluorescence correlation spectroscopy (STED-FCS).
  • Analyzed enzyme transit times through subdiffraction-sized focus spots.
  • Developed theoretical models to quantify the observed enzyme migration mechanism.

Main Results:

  • Demonstrated that active enzymes, urease and acetylcholinesterase, exhibit spontaneous migration towards lower substrate concentrations (antichemotaxis).
  • Observed two distinct enzyme transit time modes: diffusive and ballistic.
  • Correlated the ballistic transit time with the enzyme's catalytic turnover rate.

Conclusions:

  • Active enzymes employ a 'run-and-tumble' mechanism for migration, analogous to microbial foraging.
  • This biochemical information-processing algorithm could inform the design of synthetic self-propelled swimmers and nanoparticles.
  • Enzyme antichemotaxis can homogenize product concentration, particularly in environments with spatially varying reactant levels.