Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS 3 Coordination Environment Imitating Metalloid Binding Sites in Proteins
The AsIII binding of two NTA-based tripodal pseudopeptides, possessing three cysteine (ligand L1) or D- penicillamine residues (ligand L2) as potential coordinating groups for soft semimetals or metal ions, was studied by experimental (UV, CD, NMR, and ESI-MS) and theoretical (DFT) methods. All of t...
Elmentve itt :
| Szerzők: | |
|---|---|
| Dokumentumtípus: | Cikk |
| Megjelent: |
2023
|
| Sorozat: | INORGANIC CHEMISTRY
62 No. 17 |
| Tárgyszavak: | |
| doi: | 10.1021/acs.inorgchem.3c00563 |
| mtmt: | 33767799 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/28472 |
| Tartalmi kivonat: | The AsIII binding of two NTA-based tripodal pseudopeptides, possessing three cysteine (ligand L1) or D- penicillamine residues (ligand L2) as potential coordinating groups for soft semimetals or metal ions, was studied by experimental (UV, CD, NMR, and ESI-MS) and theoretical (DFT) methods. All of the experimental data, obtained with the variation of the AsIII:ligand concentration ratios or pH values in some instances, evidence the exclusive formation of species with an AsS3-type coordination mode. The UV-monitored titration of the ligands with arsenous acid at pH = 7.0 provided an absorbance data set that allowed for the determination of apparent stability constants of the forming species. The obtained stabilities (logK ' = 5.26 (AsL1) and logK ' = 3.04 (AsL2)) reflect high affinities, especially for the sterically less restricted cysteine derivative. DFT calculated structures correlate well with the spectroscopic results and, in line with the 1H NMR data, indicate a preference for the all-endo conformers resembling the AsIII environment at the semimetal binding sites in various metalloproteins. |
|---|---|
| Terjedelem/Fizikai jellemzők: | 6817-6824 |
| ISSN: | 0020-1669 |