QM/MM study of the binding of H2 to MoCu CO dehydrogenase: development and applications of improved H2 van der Waals parameters

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

The MoCu CO dehydrogenase enzyme not only transforms CO into CO2 but it can also oxidise H2. Even if its hydrogenase activity has been known for decades, a debate is ongoing on the most plausible mode for the binding of H2 to the enzyme active site and the hydrogen oxidation mechanism. In the present work, we provide a new perspective on the MoCu-CODH hydrogenase activity by improving the in silico description of the enzyme. Energy refinement—by means of the BigQM approach—was performed on the intermediates involved in the dihydrogen oxidation catalysis reported in our previously published work (Rovaletti, et al. “Theoretical Insights into the Aerobic Hydrogenase Activity of Molybdenum–Copper CO Dehydrogenase.” Inorganics 7 (2019) 135). A suboptimal description of the H2–HN(backbone) interaction was observed when the van der Waals parameters described in previous literature for H2 were employed. Therefore, a new set of van der Waals parameters is developed here in order to better describe the hydrogen–backbone interaction. They give rise to improved binding modes of H2 in the active site of MoCu CO dehydrogenase. Implications of the resulting outcomes for a better understanding of hydrogen oxidation catalysis mechanisms are proposed and discussed.

Detaljer

Författare
Enheter & grupper
Externa organisationer
  • University of Milano-Bicocca
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Teoretisk kemi

Nyckelord

Originalspråkengelska
Artikelnummer68
TidskriftJournal of Molecular Modeling
Volym27
Utgåva nummer3
StatusPublished - 2021
PublikationskategoriForskning
Peer review utfördJa