A5048192354- X-ray Diffraction in Crystallography
- Crystallization and Solubility Studies
- Lanthanide and Transition Metal Complexes
- Magnetism in coordination complexes
- Metalloenzymes and iron-sulfur proteins
- Photochemistry and Electron Transfer Studies
- Electrocatalysts for Energy Conversion
- Metal-Catalyzed Oxygenation Mechanisms
- Sulfur Compounds in Biology
- Molecular Junctions and Nanostructures
- Radioactive element chemistry and processing
- Metal-Organic Frameworks: Synthesis and Applications
- Advanced NMR Techniques and Applications
- Organic and Molecular Conductors Research
- Porphyrin and Phthalocyanine Chemistry
University of New Mexico
2022-2024
Related BAP [BAP = bis(acyl)phosphide] and Acac (Acac β-diketonate) molecules perform as robust supports for both lanthanide actinide metals. Here, a molecular bimetallic Eu2+ complex was successfully targeted isolated by employing sodium bis(mesitoyl)phosphide [Na(mesBAP)] in salt metathesis with EuI2, producing [Eu(mesBAP)2(et2o)]2 (et2o metal-coordinated diethyl ether). The corresponding Acac-Eu2+ using mesAcac– (1,3-dimesityl-1,3-propanedione), generating [Eu(mesAcac)2(et2o)]2. Both...
The electronic structure of the bis(dioxolene) bridging ligand -
A series of bis(acyl)phosphide-supported Eu complexes were synthesized (bis(acyl)phosphide = BAP). In this study, BAP ligands proved to be excellent for the synthesis both Eu3+ and Eu2+ molecular complexes. Sodium bis(mesitoyl)phosphide (Na(mesBAP)) sodium bis(2,4,6-triisopropylbenzoyl)phosphide (Na(trippBAP)) employed as ligand precursors Eu(bis(mesitoyl)phosphide)3(thf)2 (Eu(mesBAP)3(thf)2) Eu(bis(2,4,6-triisopropylbenzoyl)phosphide)3 (Eu(trippBAP)3), well complex,...
A symmetry-based model that explicitly includes the bridge fragment is used to explain a continuum of electronic structures for Kekulé-type biradicals.
X-ray absorption near-edge structure (XANES) and extended fine (EXAFS) data have been used to characterize the coordination environment for catalytic Mo site of
A combination of X-ray absorption and low-temperature electronic spectroscopies has been used to probe the geometric structures human mitochondrial amidoxime reducing component enzyme (hmARC1) in oxidized Mo(VI) reduced Mo(IV) forms. Extended fine structure analysis revealed that possesses a 5-coordinate [MoO