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Author Roy, Mahua ♦ Grazioli, Gianmarc ♦ Andricioaei, Ioan
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY ♦ CATALYSIS ♦ CHEMISTRY ♦ COORDINATES ♦ COUPLING ♦ DEGREES OF FREEDOM ♦ DIFFUSION EQUATIONS ♦ ENZYME ACTIVITY ♦ ENZYMES ♦ MOLECULAR DYNAMICS METHOD ♦ POTENTIALS ♦ REDUCTION ♦ SUBSTRATES
Abstract A novel aspect in the area of mechano-chemistry concerns the effect of external forces on enzyme activity, i.e., the existence of mechano-catalytic coupling. Recent experiments on enzyme-catalyzed disulphide bond reduction in proteins under the effect of a force applied on the termini of the protein substrate reveal an unexpected biphasic force dependence for the bond cleavage rate. Here, using atomistic molecular dynamics simulations combined with Smoluchowski theory, we propose a model for this behavior. For a broad range of forces and systems, the model reproduces the experimentally observed rates by solving a reaction-diffusion equation for a “protein coordinate” diffusing in a force-dependent effective potential. The atomistic simulations are used to compute, from first principles, the parameters of the model via a quasiharmonic analysis. Additionally, the simulations are also used to provide details about the microscopic degrees of freedom that are important for the underlying mechano-catalysis.
ISSN 00219606
Educational Use Research
Learning Resource Type Article
Publisher Date 2015-07-28
Publisher Place United States
Journal Journal of Chemical Physics
Volume Number 143
Issue Number 4


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