Show simple item record

Authordc.contributor.authorRiedel, Clement 
Authordc.contributor.authorGabizon, Ronen 
Authordc.contributor.authorWilson Moya, Christian 
Authordc.contributor.authorHamadani, Kambiz 
Authordc.contributor.authorTsekouras, Konstantinos 
Authordc.contributor.authorMarqusee, Susan 
Authordc.contributor.authorPresse, Steve 
Authordc.contributor.authorBustamante, Carlos 
Cita de ítemdc.identifier.citationNature, Volumen 517, Número 7533, págs. 227-U288, Jan 8, 2015en_US
Identifierdc.identifier.otherDOI: 10.1038/nature14043
General notedc.descriptionArtículo de publicación ISIen_US
Abstractdc.description.abstractRecent studies have shown that the diffusivity of enzymes increases in a substrate-dependent manner during catalysis1,2. Although this observation has been reported and characterized for several different systems3–10, the precise origin of this phenomenon is unknown. Calorimetric methods are often used to determine enthalpies from enzyme-catalysed reactions and can therefore provide important insight into their reaction mechanisms11,12. The ensemble averages involved in traditional bulk calorimetry cannot probe the transient effects that the energy exchanged in a reaction may have on the catalyst. Here we obtain single-molecule fluorescence correlation spectroscopy data and analyse themwithin the framework of a stochastic theory to demonstrate a mechanistic link between the enhanced diffusion of a single enzyme molecule and the heat released in the reaction. Wepropose that the heat released during catalysis generates an asymmetric pressure wave that results in a differential stress at the protein–solvent interface that transiently displaces the centre-of-mass of the enzyme (chemoacoustic effect). This novel perspective onhow enzymes respond to the energy released during catalysis suggests a possible effect of the heat of reaction on the structural integrity and internal degrees of freedom of the enzyme.en_US
Patrocinadordc.description.sponsorshipNIH R01-GM0325543 R01-GM05945 US Department of Energy, Office of Basic Energy Sciences, Division of Materials Sciences and Engineering DE-AC02-05CH11231 NSF MCB-1412259 MCB-1122225 grant NIGMS R01-GM65050 Human Frontier Science Program Burroughs-Wellcome Fund
Type of licensedc.rightsAtribución-NoComercial-SinDerivadas 3.0 Chile*
Link to Licensedc.rights.uri*
Títulodc.titleThe heat released during catalytic turnover enhances the diffusion of an enzymeen_US
Document typedc.typeArtículo de revista

Files in this item


This item appears in the following Collection(s)

Show simple item record

Atribución-NoComercial-SinDerivadas 3.0 Chile
Except where otherwise noted, this item's license is described as Atribución-NoComercial-SinDerivadas 3.0 Chile