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

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)214-217
Number of pages4
JournalChemical Physics Letters
Volume491
Issue number4-6
DOIs
Publication statusPublished - 17 May 2010

ASJC Scopus subject areas

  • General Physics and Astronomy
  • Physical and Theoretical Chemistry

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