40936-12-7Relevant articles and documents
Characterization of Spin Adducts obtained with Hydrophobic Nitrone Spin Traps
Barker, Philipp,Beckwith, Athelstan L. J.,Cherry, William R.,Huie, Reeves
, p. 1147 - 1150 (1985)
Several 5-alkyl-3,3,5-trimethylpyrrolidine 1-oxides have been prepared and their ability to trap a number of radicals has been investigated.In each case the addition to the nitrone is stereospecific and affords only one of the two possible geometric isomers of the resulting nitroxyl radical.The addition of a hydrogen atom gives nitroxyls containing two non-equivalent α-protons, the spectra of which are very similar to that observed during the red blood cell haemolysis induced by phenylhydrazine in the presence of a similar trap.A re-interpretation of the results obtained in the biological system appears to be warranted.
Surfactant-Type Catalyst for Aerobic Oxidative Coupling of Hydrazine with Thiol in Water
Ren, Xuanhe,Tang, Shanyu,Li, Longjia,Li, Jiao,Liang, Helong,Li, Ganzhong,Yang, Guanyu,Li, Heng,Yuan, Bingxin
supporting information, p. 8683 - 8690 (2019/07/08)
A series of PEG-functionalized nitrogen ligands were developed to conduct an aerobic oxidative cross-coupling reaction between alkyl- or aryl-hydrazines with thiols in water. This surfactant-type catalyst enables high efficiencies and selectivities, while tolerating a large variety of functional groups. The mother liquor is still catalytically active after five runs.
Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis
Voelkert, Martin,Koul, Surrinder,Mueller, Gernot H.,Lehnig, Manfred,Waldmann, Herbert
, p. 6902 - 6910 (2007/10/03)
The enzymatic cleavage of amino acid phenylhydrazides with the enzyme tyrosinase (EC 1.14.18.1) offers a new, mild, and selective method for C-terminal deprotection of peptides. The advantages of the described methodology are the very mild oxidative removal of the protecting group at room temperature and pH 7, a high chemo- and regioselectivity, and the availability of the biocatalyst. Even in oxygen-saturated solution, the oxidation of sensitive methionine residues was not observed. These features make the methodology suitable for the synthesis of sensitive peptide conjugates. Mechanistic data suggest that the hydrolysis of the oxidized adducts proceeds by a free-radical mechanism.