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Title

Functional and structural characterization of a membrane-bound NiFeSe Hase immobilized on an electrode with phospholipid bilayer

AuthorsGutiérrez-Sanz, Óscar ; Rüdiger Ortiz, Olaf ; Gutiérrez Sánchez, Cristina ; Olea, David ; Marqués, Marta; Lubitz, Wolfgang; Pereira, Inês A. C.; Lacey, Antonio L. de
Issue Date8-Jul-2013
Citation10th International Hydrogenase Conference (2013)
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.
DescriptionTrabajo presentado en la 10th International Hydrogenase Conference celebrada en Szeged (Hungría) del 8 al 12 de julio de 2013.
URIhttp://hdl.handle.net/10261/183505
Appears in Collections:(ICP) Comunicaciones congresos
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