2213-77-6

Upstream product

• 3646-98-8 p-cresol-2,3,5,6-d4-OD 
• 2876-03-1 2,3,5,6-d₄-p-cresol 
• 106-44-5 p-cresol 
• 13122-37-7 2,4,6-trideuteriotoluene 

Relevant academic research and scientific papers

Tunable arylative cyclization of 1,6-enynes triggered by rhodium(III)-catalyzed C-H activation

Two tunable arylative cyclizations of cyclohexadienone-containing 1,6-enynes are reported via rhodium(III)-catalyzed C-H activation of O-substituted N-hydroxybenzamides. The use of different O substituents, i.e. O-Piv and O-Me, on the directing group allows the formation of either tetracyclic isoquinolones through an N-Michael addition process or hydrobenzofurans through a C-Michael addition process. Mechanistic investigations of these two cascade reactions clearly indicated that the C-H bond cleavage process was involved in the turnover-limiting step. Furthermore, the cyclization products could be subjected to various transformations for elaborating the pharmaceutically and synthetically valuable potential. This is the first example of a rhodium(III)-catalyzed arylative cyclization reaction of 1,6-enynes, and the results extend the application realm of CpRhIII-catalyzed C-H activation cascade reactions.

Vibrational spectra and normal coordinate analysis of p-cresol and its deuterated analogs

I.r. and Raman spectra of p-cresol and its seven deuterated analogs were investigated in dilute solutions of hydrophobic solvents.Assignments of the observed i.r. and Raman bands were made on the basis of isotopic frequency shifts, Raman polarization properties, i.r. intensities and normal coordinate calculations.The calculated normal frequencies are in good agreement with the experimental ones: the average error below 1700 cm-1 is 3.8 cm-1 for 164 in-plane vibrations and 3.3 cm-1 for 59 out-of-plane vibrations.The calculated vibrational modes may be useful in analysing the vibrational spectra of tyrosine.It is suggested that several doublets due to Fermi resonance and a trio of Raman bands in the 1260-1160 cm-1 region are potential probes for the micro-environments of tyrosine side chains in proteins.