Addressing Ligand-Based Redox in Molybdenum-Dependent Methionine Sulfoxide Reductase
| Autor: | Amrit Pokhrel, Jing Yang, Martin L. Kirk, Laura J. Ingersol, Christopher A. Johnston, Andrei V. Astashkin, Khadanand Kc, Joel H. Weiner |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
inorganic chemicals
Context (language use) Ligands 010402 general chemistry 01 natural sciences Biochemistry Redox Article Catalysis law.invention chemistry.chemical_compound Colloid and Surface Chemistry Sulfite law Electron paramagnetic resonance Molybdenum biology Ligand Pulsed EPR Electron Spin Resonance Spectroscopy Active site General Chemistry 0104 chemical sciences Crystallography X-Ray Absorption Spectroscopy chemistry Methionine Sulfoxide Reductases biology.protein Methionine sulfoxide reductase Oxidation-Reduction |
| Zdroj: | J Am Chem Soc |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.9b11762 |
| Popis: | A combination of pulsed EPR, CW EPR, and XAS spectroscopies have been employed to probe the geometric and electronic structure of the E. coli periplasmic molybdenum-dependent methionine sulfoxide reductase (MsrP). (17)O and (1)H pulsed EPR spectra show that the as-isolated Mo(V) enzyme form does not possess an exchangeable H(2)O/OH(−) ligand bound to Mo as found in the sulfite oxidizing enzymes of the same family. The nature of the unusual CW EPR spectrum has been re-evaluated in light of new data on the MsrP-N45R variant and related small molecule analogs of the active site. These data point to a novel “thiol-blocked” [(PDT)Mo(V)O(S(Cys))(thiolate)](1−) structure, which is supported by new EXAFS data. We discuss these new results in the context of ligand-based and metal-based redox chemistry in the enzymatic oxygen atom transfer reaction. |
| Databáze: | OpenAIRE |
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