118058-69-8Relevant articles and documents
Visible-light-initiated manganese-catalyzed Giese addition of unactivated alkyl iodides to electron-poor olefins
Dong, Jianyang,Wang, Xiaochen,Wang, Zhen,Song, Hongjian,Liu, Yuxiu,Wang, Qingmin
supporting information, p. 11707 - 11710 (2019/10/02)
Herein, we report a mild protocol for direct visible-light-initiated Giese addition of unactivated alkyl iodides to electron-poor olefins (Michael acceptors) with catalysis by decacarbonyl dimanganese, Mn2(CO)10, an inexpensive earth-abundant-metal catalyst. This protocol is compatible with a wide array of sensitive functional groups and has a broad substrate scope with regard to both the alkyl iodide and the Michael acceptor.
Specificity of esterases and structure of prodrug esters: Reactivity of various acylated acetaminophen compounds and acetylaminobenzoated compounds
Seki,Kawaguchi,Higuchi
, p. 855 - 860 (2007/10/02)
The relative rates of enzymatically catalyzed hydrolysis of various esters of p-acetylaminobenzoic acid (APAB) and variously acylated acetaminophen (APAP) derivatives were measured. Neutral, anionic, and cationic esters were examined. The enzyme sources adopted were rat intestinal homogenate, rat liver homogenate, rat plasma, and a partly purified commercial enzyme. In both APAB and APAP esters, neutral esters were the most sensitive of the enzyme sources examined, and the sensitivity was due to the carbon chain length. The APAP esters were enzymatically more stable than the APAP esters. The relative rates of hydrolysis of these esters varied depending on the enzyme source. The ability of structure recognition was good in rat intestinal homogenate, but weak in rat plasma. These results suggest that ester prodrugs can be designed to cleave preferentially at selected sites along the pathway between absorption and disposition in the body.
