New Insights into the Berg−Holm Oxomolybdoenzyme Model
Author:
Affiliation:
1. Contribution from the School of Chemistry, University of Melbourne, Parkville, Victoria 3052, Australia, and Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Clayton, Victoria 3168, Australia
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja9900959
Reference67 articles.
1. Synthetic approach to the mononuclear active sites of molybdoenzymes: catalytic oxygen atom transfer reactions by oxomolybdenum(IV,VI) complexes with saturation kinetics and without molybdenum(V) dimer formation
2. Model for the active site of oxo-transfer molybdoenzymes: synthesis, structure, and properties
3. Model for the active sites of oxo-transfer molybdoenzymes: reactivity, kinetics, and catalysis
4. Thermodynamic fitness of molybdenum(IV,VI) complexes for oxygen-atom transfer reactions, including those with enzymic substrates
5. Thiol as an electron donor in molybdenum oxo-transferase analog reaction systems: observations by fluorine-19 NMR spectroscopy and biological implications
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