ArticleScientific reports2018
QM/MM study of the reaction mechanism of sulfite oxidase.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 28 citations in OpenAlex.
- Quantum refinement with electron diffraction and X-ray free-electron laser data: comparative study of ribonucleotide reductase dimetal site.Journal of applied crystallography · 2026Article
- Comparative Study of Aqueous Acid-Base Properties of Tungstocene and Molybdocene Complexes.Organometallics · 2026Article
- Carbon Sink Potential of Sulfur-Oxidizing Bacteria in Groundwater at Petroleum-Contaminated Sites.Microorganisms · 2025Article
- Adaptive Restraints to Accelerate Geometry Optimizations of Large Biomolecular Systems.Journal of computational chemistry · 2025Article
- Bringing Nitric Oxide to the Molybdenum World-A Personal Perspective.Molecules (Basel, Switzerland) · 2023Review
- Active Site Structures of theInorganic chemistry · 2023Article
- An unprecedented function for a tungsten-containing oxidoreductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Resonance Raman spectroscopy of pyranopterin molybdenum enzymes.Journal of inorganic biochemistry · 2022Review
- Sulfur and Phosphorus Oxyacid Radicals.The journal of physical chemistry. A · 2022Article
- Enhanced-Sampling Simulations for the Estimation of Ligand Binding Kinetics: Current Status and Perspective.Frontiers in molecular biosciences · 2022Review
- Quantum refinement with multiple conformations: application to the P-cluster in nitrogenase.Acta crystallographica. Section D, Structural biology · 2020Article
- Does the crystal structure of vanadium nitrogenase contain a reaction intermediate? Evidence from quantum refinement.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.Metal ions in life sciences · 2020Article
- On the Difference Between Additive and Subtractive QM/MM Calculations.Frontiers in chemistry · 2018Article
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sulfite oxidase is a mononuclear molybdenum enzyme that oxidises sulfite to sulfate in many organisms, including man. Three different reaction mechanisms have been suggested, based on experimental and computational studies. Here, we study all three with combined quantum mechanical (QM) and molecular mechanical (QM/MM) methods, including calculations with large basis sets, very large QM regions (803 atoms) and QM/MM free-energy perturbations. Our results show that the enzyme is set up to follow a mechanism in which the sulfur atom of the sulfite substrate reacts directly with the equatorial oxo ligand of the Mo ion, forming a Mo-bound sulfate product, which dissociates in the second step. The first step is rate limiting, with a barrier of 39-49 kJ/mol. The low barrier is obtained by an intricate hydrogen-bond network around the substrate, which is preserved during the reaction. This network favours the deprotonated substrate and disfavours the other two reaction mechanisms. We have studied the reaction with both an oxidised and a reduced form of the molybdopterin ligand and quantum-refinement calculations indicate that it is in the normal reduced tetrahydro form in this protein.
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