A5053100817- Photosynthetic Processes and Mechanisms
- Plant pathogens and resistance mechanisms
- Porphyrin Metabolism and Disorders
- Metal-Organic Frameworks: Synthesis and Applications
- RNA modifications and cancer
- RNA and protein synthesis mechanisms
- Conducting polymers and applications
- Covalent Organic Framework Applications
- Copper-based nanomaterials and applications
- Quantum Dots Synthesis And Properties
- ZnO doping and properties
- Crystallization and Solubility Studies
- Luminescence and Fluorescent Materials
- Metalloenzymes and iron-sulfur proteins
- X-ray Diffraction in Crystallography
University of Florida
2021-2024
Here, we describe the synthesis of hexameric macrocyclic aniline (MA[6]), which spontaneously assembles into coaxially conductive organic wires in its oxidized and acidified emeraldine salt (ES) form. Electrical measurements reveal that ES-MA[6] exhibits high electrical conductivity (7.5 × 10-2 S·cm-1) this is acid-base responsive. Single-crystal X-ray crystallography reveals well-defined trimeric units then stack nanotubes with regular channels, providing a potential route to synthetic are...
Abstract Queuosine (Q) is a conserved hypermodification of the wobble base tRNA containing GUN anticodons but physiological consequences Q deficiency are poorly understood in bacteria. This work combines transcriptomic, proteomic and studies to characterize Q-deficient Escherichia coli K12 MG1655 mutant. The absence led an increased resistance nickel cobalt, sensitivity cadmium, compared wild-type (WT) strain. Transcriptomic analysis WT strains, grown presence nickel, revealed that...
Plasmon-generated hot electrons in metal/oxide heterostructures have been used extensively for driving photochemistry. However, little is known about the origin of plasmon-generated holes promoting photochemical reactions. Herein, we discover that, during nonradiative plasmon decay, interband excitation rather than intraband generates energetic that enable to drive water oxidation at Au/TiO2 interface. Distinct from lukewarm via only remain on Au, are found be transferred Au into TiO2 and...
The hexameric low-pH stress response enzyme oxalate decarboxylase catalyzes the decarboxylation of mono-anion in soil bacterium Bacillus subtilis. A single protein subunit contains two Mn-binding cupin domains, and catalysis depends on Mn(III) at N-terminal site. present study suggests a mechanistic function for C-terminal Mn as an electron hole donor Mn. resulting spatial separation radical intermediates directs chemistry toward substrate. π-stacked tryptophan pair (W96/W274) links...
Oxalate decarboxylase is an Mn- and O2-dependent enzyme in the bicupin superfamily that catalyzes redox-neutral disproportionation of oxalate monoanion to form carbon dioxide formate. Its best-studied isozyme from Bacillus subtilis where it stress-induced under low pH conditions. Current mechanistic schemes assume a monodentate binding mode substrate N-terminal active site Mn ion make space for presumed O2 molecule, despite fact generally prefers bind bidentate Mn. We report on X-band...
Queuosine is a structurally unique and functionally important tRNA modification, widely distributed in eukaryotes bacteria. The final step of queuosine biosynthesis the reduction/deoxygenation epoxyqueuosine to form cyclopentene motif nucleobase. chemistry performed by characterized cobalamin-dependent QueG. However, queG gene absent from several bacteria that otherwise retain machinery. Members IPR003828 family (previously known as DUF208) have been recently identified nonorthologous...
Oxalate decarboxylase from Bacillus subtilis is a binuclear Mn-dependent acid stress response enzyme that converts the mono-anion of oxalic into formate and carbon dioxide in redox neutral unimolecular disproportionation reaction. A π-stacked tryptophan dimer, W96 W274, at interface between two monomer subunits facilitates long-range electron transfer Mn ions plays an important role catalytic mechanism. Substitution with unnatural amino 5-hydroxytryptophan leads to persistent EPR signal...