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The cage effect in the activity of [NiFeSe] hydrogenases

AuthorsLacey, Antonio L. de; Gutiérrez-Sanz, Óscar ; Marqués, Marta; Baltazar, Carla S. A.; Pereira, Inês A. C.; Soares, Claudio M.
Issue Date8-Jul-2013
Citation10th International Hydrogenase Conference (2013)
AbstractThe [NiFeSe] hvdrogcnases belong to a subgroup of the [NiFe] enzymes in which selcnocysteine is a ligand of the Ni atom in the active site instead of cysteine. The [NiFeSe] hydrogenase from Desuifilbrio arts Hildenhorough is a membrane-bound enzyme, which is anchored via a lipidic [ail placed in a region opposite to its distal [4Fe4S] cluster. We present a combined experimental and theoretical study of the catalytic activity of this ENiFeSe] bvdrugenase by HID exchange mass-spectrometry and molecular dynamics (MD) simulations_ The aim of this research is to determine how much are the specific catalytic properties of this hydrogenase influenced by the replacement of a S by Sc in the coordination of the bimetallic active site versus the changes in the protein structure surrounding the active site. Both experimental and calculated results support That a >cage effect> due to the protein structure surrounding the active site is modulating the enzymatic catalysis. In addition, we present electrochemical results of this enzyme immobilized onto gold electrodes modified ii,vith supported biornimetic membranes, thus studying the functional properties of this hydrogenase in a configuration that simulates its fn rho conditions.
DescriptionTrabajo presentado en la 10th International Hydrogenase Conference celebrada en Szeged (Hungría) del 8 al 12 de julio de 2013.
Appears in Collections:(ICP) Comunicaciones congresos
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