Enzyme leaps fuel antichemotaxis.

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Proceedings of the National Academy of Sciences of the United States of America, ISSN: 1091-6490, Vol: 115, Issue: 1, Page: 14-18

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Jee, Ah-Young; Dutta, Sandipan; Cho, Yoon-Kyoung; Tlusty, Tsvi; Granick, Steve
Proceedings of the National Academy of Sciences; NATL ACAD SCIENCES
Multidisciplinary; enzyme; chemotaxis; active matter; FCS; fluorescence correlation spectroscopy
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There is mounting evidence that enzyme diffusivity is enhanced when the enzyme is catalytically active. Here, using superresolution microscopy [stimulated emission-depletion fluorescence correlation spectroscopy (STED-FCS)], we show that active enzymes migrate spontaneously in the direction of lower substrate concentration ("antichemotaxis") by a process analogous to the run-and-tumble foraging strategy of swimming microorganisms and our theory quantifies the mechanism. The two enzymes studied, urease and acetylcholinesterase, display two families of transit times through subdiffraction-sized focus spots, a diffusive mode and a ballistic mode, and the latter transit time is close to the inverse rate of catalytic turnover. This biochemical information-processing algorithm may be useful to design synthetic self-propelled swimmers and nanoparticles relevant to active materials. Executed by molecules lacking the decision-making circuitry of microorganisms, antichemotaxis by this run-and-tumble process offers the biological function to homogenize product concentration, which could be significant in situations when the reactant concentration varies from spot to spot.