58755-57-0Relevant articles and documents
Visible-light assisted of nano Ni/g-C3N4 with efficient photocatalytic activity and stability for selective aerobic C?H activation and epoxidation
Akrami, Zahra,Hosseini-Sarvari, Mona
supporting information, (2020/10/13)
A selective, economical, and ecological protocol has been described for the oxidation of methyl arenes and their analogs to the corresponding carbonyl compounds and epoxidation reactions of alkenes with molecular oxygen (O2) or air as a green oxygen source, under mild reaction conditions. The nano Ni/g-C3N4 exhibited high photocatalytic activity, stability, and selectivity in the C?H activation of methyl arenes, methylene arenes, and epoxidation of various alkenes under visible- light irradiation without the use of an oxidizing agent and under base free conditions.
Iterative design of a biomimetic catalyst for amino acid thioester condensation
Wu, Huabin,Handoko,Raj, Monika,Arora, Paramjit S.
supporting information, p. 5122 - 5125 (2017/11/06)
Herein, the design of a catalyst that combines lessons learned from peptide biosynthesis, enzymes, and organocatalysts is described. The catalyst features a urea scaffold for carbonyl recognition and elements of nucleophilic catalysis. In the presence of 10 mol % of the organocatalyst, the rate of peptide bond formation is accelerated by 10000-fold over the uncatalyzed reaction between Fmoc-amino acid thioesters and amino acid methyl esters.
Novel pseudopeptides incorporating a benzodiazepine-based turn mimetic - Targeting Mycobacterium tuberculosis ribonucleotide reductase
Nurbo, Johanna,Ericsson, Daniel J.,Rosenstr?m, Ulrika,Muthas, Daniel,Jansson, Anna M.,Lindeberg, Gunnar,Unge, Torsten,Karlén, Anders
, p. 1992 - 2000 (2013/05/08)
Peptides mimicking the C-terminus of the small subunit (R2) of Mycobacterium tuberculosis ribonucleotide reductase (RNR) can compete for binding to the large subunit (R1) and thus inhibit RNR activity. Moreover, it has been suggested that the binding of t