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               <dc:title>Intrinsic enzymatic properties modulate the self-propulsion of micromotors</dc:title>
               <dc:creator>Arqué, Xavier</dc:creator>
               <dc:creator>Romero Rivera, Adrian</dc:creator>
               <dc:creator>Feixas Geronès, Ferran</dc:creator>
               <dc:creator>Patiño, Tania</dc:creator>
               <dc:creator>Osuna Oliveras, Sílvia</dc:creator>
               <dc:creator>Sánchez, Samuel</dc:creator>
               <dc:subject>Cinètica enzimàtica</dc:subject>
               <dc:subject>Enzyme kinetics</dc:subject>
               <dc:subject>Catàlisi</dc:subject>
               <dc:subject>Catalysis</dc:subject>
               <dc:description>Bio-catalytic micro- and nanomotors self-propel by the enzymatic conversion of substrates&#xd;
into products. Despite the advances in the field, the fundamental aspects underlying enzymepowered self-propulsion have rarely been studied. In this work, we select four enzymes&#xd;
(urease, acetylcholinesterase, glucose oxidase, and aldolase) to be attached on silica&#xd;
microcapsules and study how their turnover number and conformational dynamics affect the&#xd;
self-propulsion, combining both an experimental and molecular dynamics simulations&#xd;
approach. Urease and acetylcholinesterase, the enzymes with higher catalytic rates, are the&#xd;
only enzymes capable of producing active motion. Molecular dynamics simulations reveal&#xd;
that urease and acetylcholinesterase display the highest degree of flexibility near the active&#xd;
site, which could play a role on the catalytic process. We experimentally assess this&#xd;
hypothesis for urease micromotors through competitive inhibition (acetohydroxamic acid)&#xd;
and increasing enzyme rigidity (β-mercaptoethanol). We conclude that the conformational&#xd;
changes are a precondition of urease catalysis, which is essential to generate self-propulsio</dc:description>
               <dc:description>The research leading to these results has received funding from the Spanish MINECO for&#xd;
grants CTQ2015-68879-R (MICRODIA) and CTQ2015-72471-EXP (Enzwim). T.P. thanks&#xd;
MINECO for the Juan de la Cierva fellowship (FJCI-2015-25578). A.R.-R. thanks the&#xd;
Generalitat de Catalunya for PhD fellowship (2015-FI-B-00165). F.F. thanks the European&#xd;
Community for MSCA-IF-2014-EF-661160-MetAccembly grant. S.O. thanks funding from&#xd;
the European Research Council (ERC) under the European Union’s Horizon 2020 research&#xd;
and innovation programme (ERC-2015-StG-679001). F.F., A.R.-R., and S.O. thank the&#xd;
Generalitat de Catalunya for grup emergent 2017 SGR-1707. S.S. acknowledges Foundation&#xd;
BBVA for the MEDIROBOTS project and the CERCA program by the Generalitat de&#xd;
Catalunya</dc:description>
               <dc:date>2019-06-27</dc:date>
               <dc:type>info:eu-repo/semantics/article</dc:type>
               <dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
               <dc:type>peer-reviewed</dc:type>
               <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-019-10726-8</dc:relation>
               <dc:relation>info:eu-repo/semantics/altIdentifier/issn/2041-1723</dc:relation>
               <dc:relation>info:eu-repo/grantAgreement/EC/H2020/661160/EU/Accelerating metal-directed assembly, recognition and catalysis with computational methods/MetAccembly</dc:relation>
               <dc:rights>Attribution 4.0 International</dc:rights>
               <dc:rights>http://creativecommons.org/licenses/by/4.0/</dc:rights>
               <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
               <dc:publisher>Nature Research</dc:publisher>
               <dc:source>Nature Communications, 2019, vol. 10, art. núm. 2826</dc:source>
               <dc:source>Articles publicats (D-Q)</dc:source>
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