A5075358131- Hemoglobin structure and function
- Metal-Catalyzed Oxygenation Mechanisms
- Nitric Oxide and Endothelin Effects
- Porphyrin and Phthalocyanine Chemistry
- Catalysis and Oxidation Reactions
- Heme Oxygenase-1 and Carbon Monoxide
- Catalytic Processes in Materials Science
- Porphyrin Metabolism and Disorders
- Photosynthetic Processes and Mechanisms
- Cassava research and cyanide
- Biochemical and Molecular Research
- Magnetism in coordination complexes
- Ammonia Synthesis and Nitrogen Reduction
- Advanced oxidation water treatment
- Sulfur Compounds in Biology
- Polyamine Metabolism and Applications
- Plant nutrient uptake and metabolism
- Electron Spin Resonance Studies
- RNA and protein synthesis mechanisms
- Microbial Fuel Cells and Bioremediation
- Neonatal Health and Biochemistry
- Enzyme Structure and Function
- Zeolite Catalysis and Synthesis
- Trace Elements in Health
- Radioactive element chemistry and processing
University of Michigan
2018-2024
Rev-Erbβ is a nuclear receptor that couples circadian rhythm, metabolism, and inflammation. Heme binding to the protein modulates its function as repressor, stability, ability bind other proteins, activity in gas sensing. binds Fe3+-heme more tightly than Fe2+-heme, suggesting activities may be regulated by heme redox state. Yet, this critical role of chemistry defining protein's resting state unknown. We demonstrate electrochemical whole-cell electron paramagnetic resonance experiments...
Cupredoxins are copper-dependent electron-transfer proteins that can be categorized as blue, purple, green, and red depending on the spectroscopic properties of Cu(II) bound forms. Interestingly, despite significantly different first coordination spheres nuclearity, all cupredoxins share a common Greek Key β-sheet fold. We have previously reported design copper protein within completely distinct three-helical bundle protein, α3DChC2.(1) While this demonstrated β-barrel fold was not requisite...
Manganese porphyrins are used as catalysts in the oxidation of olefins and nonactivated hydrocarbons. Key to these reactions high-valent Mn-(di)oxo species, for which [Mn(Porph)(X)] serve precursors. To elucidate their properties, it is crucial understand interaction Mn center with porphyrin ligand. Our study focuses on simple high-spin [MnIII(TPP)X] (X = F, Cl, I, Br) complexes emphasis spectroscopic properties [MnIII(TPP)Cl], using variable-temperature variable-field magnetic circular...
Coupled dinuclear copper oxygen cores (Cu2 O2 ) featured in type III proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for transport and substrate oxidation many organisms. μ-1,2-cis peroxido dicopper (C P) have been proposed as key structures the early stages of binding these proteins; their reversible isomerization to other Cu2 directly relevant enzyme function. Despite relevance such species broader interest properties reactivity bimetallic C P biological synthetic systems,...
Summary Molecules with nitrogen-nitrogen (N-N) bonds constitute a large group of clinically important drugs, and various synthetic approaches have been developed to construct functional groups like hydrazines, diazos, pyrazoles, N-nitrosos. While hundreds N-N-containing specialized natural metabolites also discovered, little is known about the underlying enzymatic mechanisms that evolved for N-N bond formation. In order directly form single N(sp 3 )-N(sp ) bond, enzymes must reverse typical...
-Nitroso compounds (RNO, R = alkyl and aryl) are byproducts of drug metabolism bind to heme proteins, their heme-RNO adducts isoelectronic ferrous nitroxyl (NO
Abstract Coupled dinuclear copper oxygen cores (Cu 2 O ) featured in type III proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for transport and substrate oxidation many organisms. μ ‐1,2‐ cis peroxido dicopper ( C P have been proposed as key structures the early stages of binding these proteins; their reversible isomerization to other Cu directly relevant enzyme function. Despite relevance such species broader interest properties reactivity bimetallic biological synthetic...
Abstract Rev-Erbβ is a nuclear receptor that couples circadian rhythm, metabolism, and inflammation. 1-7 Heme binding to the protein modulates its function as repressor, stability, ability bind other proteins, activity in gas sensing. 8-11 binds Fe 3+ -heme tighter than 2+ -heme, suggesting activities may be regulated by heme redox state. 9 Yet, this critical role of chemistry defining protein’s resting state unknown. We demonstrate electrochemical whole-cell electron paramagnetic resonance...