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.

Rovaletti, A., Greco, C., & Ryde, U. (2021). QM/MM study of the binding of H2 to MoCu CO dehydrogenase: development and applications of improved H2 van der Waals parameters. JOURNAL OF MOLECULAR MODELING, 27(3) [10.1007/s00894-020-04655-3].

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

Rovaletti, Anna
Primo
;
Greco, Claudio
;
2021

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.
Articolo in rivista - Articolo scientifico
Scientifica
BigQM approach; Force field parametrization; H2 oxidation; Hydrogenases; MoCu CO dehydrogenase; QM/MM;
English
Rovaletti, A., Greco, C., & Ryde, U. (2021). QM/MM study of the binding of H2 to MoCu CO dehydrogenase: development and applications of improved H2 van der Waals parameters. JOURNAL OF MOLECULAR MODELING, 27(3) [10.1007/s00894-020-04655-3].
Rovaletti, A; Greco, C; Ryde, U
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/10281/301545
Citazioni
  • Scopus 2
  • ???jsp.display-item.citation.isi??? 3
Social impact