English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/183505
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

DC FieldValueLanguage
dc.contributor.authorGutiérrez-Sanz, Óscar-
dc.contributor.authorRüdiger Ortiz, Olaf-
dc.contributor.authorGutiérrez Sánchez, Cristina-
dc.contributor.authorOlea, David-
dc.contributor.authorMarqués, Marta-
dc.contributor.authorLubitz, Wolfgang-
dc.contributor.authorPereira, Inês A. C.-
dc.contributor.authorLacey, Antonio L. de-
dc.identifier.citation10th International Hydrogenase Conference (2013)-
dc.descriptionTrabajo presentado en la 10th International Hydrogenase Conference celebrada en Szeged (Hungría) del 8 al 12 de julio de 2013.-
dc.description.abstractThe interaction of redox enzymes with electrodes is very interesting for its catalytic mechanisms study and for bioelectronics applications. The efficiency of the electron transport is better with soluble than membrane proteins due to the higher structure stability of the first one', The studies of membrane proteins in their environment help us to understand the function of membranes in the enzyme activity. The NiFcSe hydrogenase (I WO from Destilforibrio Hildenhorough is a membrane-bound protein which produces Fig very efficiently and is very quickly reactivated after oxygen exposure. The structure and activity stability on this Hass depends of lipids or detergent presence, Our laboratory has developed a strategy far immobilize membrane proteins efficiently on an electrode. Thanks to three different techniques we have characterized this imrylobilization. We have used atomic force microscopy (AFM) to study the structure'. Surface-enhanced infrared absorption (SEIRA) spectrotlectrochernistry allowed to study sensitive cbaracterization of the chemical structure at the electrode interface while driving the electrocatalytie activity of the Flase. Electrochemistry messurements were done in an anaerobic chamber to study the activity of this enzyme in presence of oxygen and monoxide carbon.-
dc.description.sponsorshipThis work was supported by Acción Integrada Hispano-Lusa AIB 2010-P1-00367 and to Spanish Ministerio de Ciencia (Project CTQ2009-12649)-
dc.titleFunctional and structural characterization of a membrane-bound NiFeSe Hase immobilized on an electrode with phospholipid bilayer-
dc.typepóster de congreso-
dc.description.versionPeer Reviewed-
dc.contributor.funderMinisterio de Ciencia e Innovación (España)-
Appears in Collections:(ICP) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show simple item record

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.