DFT-modeling of the tungsten (V) cofactor of hyperthermophilic Pyrococcus furiosus tungsto-bispterin enzyme via the calculated EPR parameters

Ricardo Veloso-Bahamonde, Rodrigo Ramirez-Tagle, Ramiro Arratia-Pérez

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

1 Cita (Scopus)

Resumen

Here we report a DFT relativistic scalar and spin-orbit study that considers the structural optimization of the complete tungsten (V) cofactor by studying the paramagnetic site of the Pyrococcus furiosus tungsto-bispterin enzyme. The best-fit superimposed X-ray structure shows an important similarity with the aldehyde ferredoxin oxidoreductase (1AOR) structure, and, the W(V) cofactor exhibits a Kramers doublet as the ground state, which agrees with the EPR observations. We conclude that it is quite necessary to include relativistic scalar and spin-orbit effects to describe the whole tungsten (V) cofactor in the P. furiosus tungsto-bispterin enzyme.

Idioma originalInglés
Páginas (desde-hasta)214-217
Número de páginas4
PublicaciónChemical Physics Letters
Volumen491
N.º4-6
DOI
EstadoPublicada - 17 may. 2010

Áreas temáticas de ASJC Scopus

  • Física y Astronomía General
  • Química física y teórica

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