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dc.contributor.authorGutiérrez-Sanz, Óscar-
dc.contributor.authorMarqués, Marta-
dc.contributor.authorPereira, Inês A. C.-
dc.contributor.authorLópez de Lacey, Antonio-
dc.contributor.authorLubitz, Wolfgang-
dc.contributor.authorRüdiger Ortiz, Olaf-
dc.date.accessioned2019-06-04T12:35:27Z-
dc.date.available2019-06-04T12:35:27Z-
dc.date.issued2013-08-05-
dc.identifier.citationJournal of Physical Chemistry Letters 4(17): 2794- 2798 (2013)-
dc.identifier.issn1948-7185-
dc.identifier.urihttp://hdl.handle.net/10261/183293-
dc.description.abstractElectrochemical SEIRA is the method of choice for characterizing a lipid-bilayer-anchored, membrane-bound hydrogenase immobilized on a gold electrode. This setup allows the study of the enzyme under conditions mimicking its natural environment. A single experiment provides all of the crucial spectroscopic information relating to the protein orientation, active site of the protein, and the lipid bilayer and also direct electrochemical determination of the catalytic H2 oxidation by the enzyme.-
dc.description.sponsorshipThis work has been supported by the Max Planck Society and the Spanish MINECO (project CTQ2012-32448). O.G.-S. thanks the MINECO for a FPI grant.-
dc.publisherAmerican Chemical Society-
dc.rightsclosedAccess-
dc.subjectSEIRA-
dc.subjectPhospholipid bilayer membranes-
dc.subjectHydrogenase-
dc.subjectProtein film electrochemistry-
dc.titleOrientation and function of a membrane-bound enzyme monitored by electrochemical surface-enhanced infrared absorption spectroscopy-
dc.typeartículo-
dc.identifier.doihttp://dx.doi.org/10.1021/jz4013678-
dc.relation.publisherversionhttps://doi.org/10.1021/jz4013678-
dc.date.updated2019-06-04T12:35:27Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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