36475-13-5Relevant articles and documents
Mechanistic studies on intramolecular C-H trifluoromethoxylation of (hetero)arenes via OCF3-migration
Lee, Katarzyna N.,Lei, Zhen,Morales-Rivera, Cristian A.,Liu, Peng,Ngai, Ming-Yu
, p. 5599 - 5605 (2016)
The one-pot two-step intramolecular aryl and heteroaryl C-H trifluoromethoxylation recently reported by our group has provided a general, scalable, and operationally simple approach to access a wide range of unprecedented and valuable OCF3-containing building blocks. Herein we describe our investigations to elucidate its reaction mechanism. Experimental data indicate that the O-trifluoromethylation of N-(hetero)aryl-N-hydroxylamine derivatives is a radical process, whereas the OCF3-migration step proceeds via a heterolytic cleavage of the N-OCF3 bond followed by rapid recombination of a short-lived ion pair. Computational studies further support the proposed ion pair reaction pathway for the OCF3-migration process. We hope that the current study would provide useful insights for the development of new transformations using versatile N-(hetero)aryl-N-hydroxylamine synthons.
Live-Cell Protein Modification by Boronate-Assisted Hydroxamic Acid Catalysis
Adamson, Christopher,Kajino, Hidetoshi,Kanai, Motomu,Kawashima, Shigehiro A.,Yamatsugu, Kenzo
supporting information, p. 14976 - 14980 (2021/09/29)
Selective methods for introducing protein post-translational modifications (PTMs) within living cells have proven valuable for interrogating their biological function. In contrast to enzymatic methods, abiotic catalysis should offer access to diverse and new-to-nature PTMs. Herein, we report the boronate-assisted hydroxamic acid (BAHA) catalyst system, which comprises a protein ligand, a hydroxamic acid Lewis base, and a diol moiety. In concert with a boronic acid-bearing acyl donor, our catalyst leverages a local molarity effect to promote acyl transfer to a target lysine residue. Our catalyst system employs micromolar reagent concentrations and affords minimal off-target protein reactivity. Critically, BAHA is resistant to glutathione, a metabolite which has hampered many efforts toward abiotic chemistry within living cells. To showcase this methodology, we installed a variety of acyl groups inE. colidihydrofolate reductase expressed within human cells. Our results further establish the well-known boronic acid-diol complexation as abona fidebio-orthogonal reaction with applications in chemical biology and in-cell catalysis.
Regioselective installation of fluorosulfate (-OSO2F) functionality into aromatic C(sp2)-H bonds for the construction of: Para-amino-arylfluorosulfates
Fang, Wan-Yin,Zha, Gao-Feng,Zhao, Chuang,Qin, Hua-Li
supporting information, p. 6273 - 6276 (2019/06/07)
The construction of para-amino-arylfluorosulfates was achieved through installation of fluorosulfate (-OSO2F) functionality into aromatic C(sp2)-H bonds by the reaction of N-arylhydroxylamine with sulfuryl fluoride (SO2Fs
