16183-32-7Relevant articles and documents
Single source precursor synthesized CuS nanoparticles for NIR phototherapy of cancer and photodegradation of organic carcinogen
Arshad, Mehwish,Wang, Zhaojie,Nasir, Jamal Abdul,Amador, Eric,Jin, Mingwu,Li, Haibin,Chen, Zhigang,Rehman, Zia ur,Chen, Wei
, (2021)
Herein, we report cost effective and body compatible CuS nanoparticles (NPs) derived from a single source precursor as photothermal agent for healing deep cancer and photocatalytic remediation of organic carcinogens. These NPs efficiently kill MCF7 cells
Rhodium catalysts with cofactor mimics for the biomimetic reduction of CN bonds
Chen, Fushan,Deng, Li,Dong, Wenjin,Tang, Jie,Xian, Mo
, p. 5564 - 5569 (2021/08/25)
A strategy based on the cooperation between metal and bonded cofactor mimics was applied to the transfer hydrogenation of CN bonds. We designed and synthesized a rhodium complex containing a 1,3-dimethylbenzoimidazole moiety, which could transfer hydride from a rhodium center to imine substrates in a biomimetic way. Under both transfer hydrogenation and reductive amination reaction conditions, the catalyst exhibited good selectivity towards CN bonds. With the catalyst, 34 imines were transfer hydrogenated to corresponding amines and a key intermediate of retigabine was prepared via reductive amination in a greener way. According to the NMR observations and isotope experiments, a plausible mechanism for this biomimetic reduction of CN bonds were proposed.
Bio-inspired catalytic imine reduction by rhodium complexes with tethered hantzsch pyridinium groups: Evidence for direct hydride transfer from dihydropyridine to metal-activated substrate
McSkimming, Alex,Bhadbhade, Mohan M.,Colbran, Stephen B.
, p. 3411 - 3416 (2013/05/08)
Inspired by Nature: A conceptually new design for a catalyst, combining a metal center abutted to an organic hydride donor, is demonstrated for the formate-driven transfer hydrogenation of imines under ambient conditions. A key step, transfer of hydride from the organohydride donor to the metal-polarized substrate, mirrors that in metallo-(de)hydrogenase enzymes.