Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/183061
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

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

AutorGutiérrez-Sanz, Óscar CSIC ORCID; Marques, Marta C.; Baltazar, Carla S. A.; Fernández, Víctor M.; Soares, Claudio M.; Pereira, Inês A. C.; López de Lacey, Antonio CSIC ORCID
Palabras claveSelenocysteine
Enzyme kinetics
Isotope exchange
Molecular dynamics
Hydrogenase
Fecha de publicaciónabr-2013
EditorSpringer Nature
CitaciónJournal of Biological Inorganic Chemistry 18(4): 419-427 (2013)
ResumenA 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.
Versión del editorhttps://doi.org/10.1007/s00775-013-0986-4
URIhttp://hdl.handle.net/10261/183061
DOI10.1007/s00775-013-0986-4
ISSN0949-8257
E-ISSN1432-1327
Aparece en las colecciones: (ICP) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

CORE Recommender

SCOPUSTM   
Citations

21
checked on 12-mar-2024

WEB OF SCIENCETM
Citations

20
checked on 22-feb-2024

Page view(s)

170
checked on 17-mar-2024

Download(s)

30
checked on 17-mar-2024

Google ScholarTM

Check

Altmetric

Altmetric


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.