Fluorine NMR studies of the human carbonic anhydrase–3,5-difluorobenzenesulfonamide complex
✍ Scribed by D. L. Veenstra; J. T. Gerig
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 274 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0749-1581
No coin nor oath required. For personal study only.
✦ Synopsis
Fluorine and nitrogen-15 NMR experiments are described which show that 3,5-diÑuorobenzenesulfonamide binds to human carbonic anhydrase I in a 1 : 1 complex, that the bound inhibitor is present as an anion and that the aromatic ring of the inhibitor undergoes rapid rotation in the complex in spite of likely interactions with the aromatic ring of Phe-91 which are strong enough to give an appreciable 19FM1HN NOE. A previously predicted enhancement of binding by Ñuorination of the inhibitor was conÐrmed.
1998 John Wiley & ( Sons, Ltd.
📜 SIMILAR VOLUMES
F NMR / EXSY / Kinetics of ligand exchange / Bailar and Ra ˆy-Dutt mechanisms The rates of intramolecular rearrangement of the meridional isomer of the metal tris-chelate complex [Ga(fox) 3 , fox = 5fluoro-8-hydroxyquinoline] in DMF solution were measured using 1D NMR line shape analysis and 2D EXS
## Abstract The ^295^Pt and ^205^Tl NMR chemical shifts of the complexes [(NC)~5~PtTl(CN)~__n__~]^__n__−^ __n__=0–3, and of the related system [(NC)~5~PtTlPt(CN)~5~]^3−^ have been computationally investigated. It is demonstrated that based on relativistically optimized geometries, by applying an