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The heat released during catalytic turnover enhances the diffusion of an enzyme

Author

Listed:
  • Clement Riedel

    (California Institute for Quantitative Biosciences, QB3, University of California)

  • Ronen Gabizon

    (California Institute for Quantitative Biosciences, QB3, University of California)

  • Christian A. M. Wilson

    (California Institute for Quantitative Biosciences, QB3, University of California
    Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, 1058 Santiago, Chile)

  • Kambiz Hamadani

    (California Institute for Quantitative Biosciences, QB3, University of California
    Present address: Department of Chemistry and Biochemistry, California State University San Marcos, California 92078, USA.)

  • Konstantinos Tsekouras

    (Indiana University-Purdue University Indianapolis (IUPUI))

  • Susan Marqusee

    (California Institute for Quantitative Biosciences, QB3, University of California
    University of California)

  • Steve Pressé

    (Indiana University-Purdue University Indianapolis (IUPUI)
    Indiana University School of Medicine)

  • Carlos Bustamante

    (California Institute for Quantitative Biosciences, QB3, University of California
    University of California
    University of California, Berkeley
    University of California)

Abstract

It has been traditionally assumed that the heat released during a single enzymatic catalytic event does not perturb the enzyme in any way; however, here single-molecule fluorescence correlation spectroscopy is used to show that, for enzymes that catalyse chemical reactions with large reaction enthalpies, the heat released at the protein's active site during catalysis transiently displaces the protein's centre-of-mass, essentially giving rise to a recoil effect that propels the enzyme.

Suggested Citation

  • Clement Riedel & Ronen Gabizon & Christian A. M. Wilson & Kambiz Hamadani & Konstantinos Tsekouras & Susan Marqusee & Steve Pressé & Carlos Bustamante, 2015. "The heat released during catalytic turnover enhances the diffusion of an enzyme," Nature, Nature, vol. 517(7533), pages 227-230, January.
    • Handle: RePEc:nat:nature:v:517:y:2015:i:7533:d:10.1038_nature14043
    DOI: 10.1038/nature14043
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    Cited by:

    1. Andrea Testa & Mirco Dindo & Aleksander A. Rebane & Babak Nasouri & Robert W. Style & Ramin Golestanian & Eric R. Dufresne & Paola Laurino, 2021. "Sustained enzymatic activity and flow in crowded protein droplets," Nature Communications, Nature, vol. 12(1), pages 1-8, December.

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