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Chemoselective hydrogenation of functionalized nitroarenes decorated with one or more reducible groups still remains a challenge. Herein we developed a novel hybrid non-noble iron-based nanocatalyst (named as FeS2/NSC) in a straightforward and cost-effective procedure. Comprehensive characterizations reveal that single phase pyrite FeS2 nanoparticles with precisely defined composition and uniform size were homogeneously dispersed on N,S-codoped porous carbon with large specific surface area, porous channel and high pore volume. The resultant catalyst FeS2/NSC demonstrated superior activity for hydrogenation of functionalized nitroarenes with good tolerance of various functional groups using water as a sustainable and green solvent. Compared with bulk pyrite FeS2 and other non-noble metal-based heterogeneous catalysts reported in the literature, a remarkably enhanced activity was observed under milder reaction conditions. More importantly, the catalyst FeS2/NSC displayed exclusive chemoselectivity to the reduction of nitro group for nitroarenes bearing varying readily reducible groups. Control experiments and DFT calculations reveal that, owing to the large electronegative N and S atoms incorporation into the carbon, the FeS2/NSC not only had a preferential adsorption of nitro group but also had a strong interaction between FeS2 nanoparticles and N,S-codoped porous carbon, which substantially boosted the catalytic activity, chemoselectivity, and stability as well.
This article was published in the following journal.
Selective hydrogenation of nitroarenes to arylamines is a great chal-lenge due to the complicated mechanism and competitive hydro-genation of reducible functional groups. Isolated single atomic site c...
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Molecules that contain multiple active sites which are used to catalyze more than one enzymatic reaction. Proteins in this class generally contain multiple active sites within a single peptide chain and may also contain more than one enzymatically active subunit. They are distinguished from MULTIENZYME COMPLEXES in that their subunits are not found as distinct enzymes.
A family of enzymes that catalyze the stereoselective, regioselective, or chemoselective syn-dehydrogenation reactions. They function by a mechanism that is linked directly to reduction of molecular OXYGEN.
Addition of hydrogen to a compound, especially to an unsaturated fat or fatty acid. (From Stedman, 26th ed)
Single preparations containing two or more active agents, for the purpose of their concurrent administration as a fixed dose mixture.
Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.