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dc.contributor.authorLacey, Antonio L. dees_ES
dc.contributor.authorGutiérrez-Sanz, Óscares_ES
dc.contributor.authorNatale, Paoloes_ES
dc.contributor.authorMárquez, Ileana F.es_ES
dc.contributor.authorMarques, Marta C.es_ES
dc.contributor.authorZacarias, Soniaes_ES
dc.contributor.authorPita, Marcoses_ES
dc.contributor.authorPereira, Inês A. C.es_ES
dc.contributor.authorLópez-Montero, Ivánes_ES
dc.contributor.authorVélez, Mariselaes_ES
dc.identifier.citationXXIV International Symposium on Bioelectrochemistry and Bioenergetics (2017)es_ES
dc.descriptionTrabajo presentado en el XXIV International Symposium on Bioelectrochemistry and Bioenergetics (BES 2017), celebrado en Lyon del 3 al 7 de julio de 2017.es_ES
dc.description.abstractCells generate energy by coupling a proton gradient across a phospholipid bilayer membrane with the activity of a cross-membrane ATP synthase enzyme. In an effort to mimic this process in an artificial environment, we show that ATP can be efficiently produced starting from molecular hydrogen as a fuel. The proton concentration in an electrode/phospholipid bilayer interface can be controlled and monitorised electrochemically by immobilizing the membrane-bound [NiFeSe]-hydrogenase from Desulfovibrio vulgaris Hildenborough.1 The electro-enzymatic oxidation of H2 generated a proton gradient across the supported biomimetic membrane that can be coupled to the in vitro synthesis of ATP by reconstituting ATP-synthase from E. coli on the biomimetic system.2es_ES
dc.titleATP synthesis coupled to the electroenzymatic activity of a hydrogenase immobilized at an electrode/biomimetic membrane interfacees_ES
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