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

Clement Riedel, Ronen Gabizon, Christian A. M. Wilson, Kambiz Hamadani, Konstantinos Tsekouras, Susan Marqusee, Steve Pressé () and Carlos Bustamante ()
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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
Kambiz Hamadani: California Institute for Quantitative Biosciences, QB3, University of California
Konstantinos Tsekouras: Indiana University-Purdue University Indianapolis (IUPUI)
Susan Marqusee: California Institute for Quantitative Biosciences, QB3, University of California
Steve Pressé: Indiana University-Purdue University Indianapolis (IUPUI)
Carlos Bustamante: California Institute for Quantitative Biosciences, QB3, University of California

Nature, 2015, vol. 517, issue 7533, 227-230

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.

Date: 2015
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DOI: 10.1038/nature14043

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