A5002225236- Metal-Catalyzed Oxygenation Mechanisms
- Electron Spin Resonance Studies
- Microbial metabolism and enzyme function
- Nanocluster Synthesis and Applications
- CO2 Reduction Techniques and Catalysts
- Heme Oxygenase-1 and Carbon Monoxide
- Magnetism in coordination complexes
- Nitric Oxide and Endothelin Effects
- Vanadium and Halogenation Chemistry
- Metalloenzymes and iron-sulfur proteins
- Photosynthetic Processes and Mechanisms
- Advanced oxidation water treatment
University of Alabama
2021-2024
The human copper-binding protein metallothionein-3 (MT-3) can reduce Cu(II) to Cu(I) and form a polynuclear
3-mercaptopropionate (3MPA) dioxygenase (MDO) is a mononuclear nonheme iron enzyme that catalyzes the O
3-Mercaptopropionic acid (3MPA) dioxygenase (MDO) is a non-heme Fe(II)/O2-dependent oxygenase that catalyzes the oxidation of thiol-substrates to yield corresponding sulfinic acid. Hydrogen-bonding interactions between Fe-site and conserved set three outer-sphere residues (Ser–His–Tyr) play an important catalytic role in mechanism this enzyme. Collectively referred as SHY-motif, functional these remains poorly understood. Here, catalytically inactive Fe(III)-MDO precomplexed with 3MPA was...