English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/183061
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Influence of the protein structure surrounding the active site on the catalytic activity of [NiFeSe] hydrogenases

AuthorsGutiérrez-Sanz, Óscar ; Marques, Marta C.; Baltazar, Carla S. A.; Fernández, Víctor M.; Soares, Claudio M.; Pereira, Inês A. C.; Lacey, Antonio L. de
Enzyme kinetics
Isotope exchange
Molecular dynamics
Issue DateApr-2013
CitationJournal of Biological Inorganic Chemistry 18(4): 419-427 (2013)
AbstractA combined experimental and theoretical study of the catalytic activity of a [NiFeSe] hydrogenase has been performed by H/D exchange mass spectrometry and molecular dynamics simulations. Hydrogenases are enzymes that catalyze the heterolytic cleavage or production of H2. The [NiFeSe] hydrogenases belong to a subgroup of the [NiFe] enzymes in which a selenocysteine is a ligand of the nickel atom in the active site instead of cysteine. The aim of this research is to determine how much the specific catalytic properties of this hydrogenase are influenced by the replacement of a sulfur by selenium in the coordination of the bimetallic active site versus the changes in the protein structure surrounding the active site. The pH dependence of the D2/H+ exchange activity and the high isotope effect observed in the Michaelis constant for the dihydrogen substrate and in the single exchange/double exchange ratio suggest that a “cage effect” due to the protein structure surrounding the active site is modulating the enzymatic catalysis. This “cage effect” is supported by molecular dynamics simulations of the diffusion of H2 and D2 from the outside to the inside of the protein, which show different accumulation of these substrates in a cavity next to the active site.
Publisher version (URL)https://doi.org/10.1007/s00775-013-0986-4
Appears in Collections:(ICP) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

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