1462-61-9Relevant academic research and scientific papers
A Broader-scope Analysis of the Catalytic Reduction of Nitrophenols and Azo Dyes with Noble Metal Nanoparticles
Shultz, Lorianne R.,Hu, Lin,Preradovic, Konstantin,Beazley, Melanie J.,Feng, Xiaofeng,Jurca, Titel
, p. 2590 - 2595 (2019)
In addition to the broad environmental implications associated with the removal of nitroaromatics from industrial effluent, the catalytic reduction of 4-nitrophenol (4NP) has emerged as a benchmark model for quantifying catalytic activity of metal nanoparticles. Here we present a series of noble metal nanoparticles immobilized on amorphous carbon (Au@C, Ag@C, Pt@C and Pd@C). All materials show competitive catalytic activity over 4NP, amino-substituted nitrophenols (ANPs) and azo dyes. Overall, Pd@C exhibits superior activity that increases further when exposed to recycling protocol. Moreover, testing all materials synthesized over a broader substrate scope with added functionalities reveals inconsistencies in the prognosticating ability of the ubiquitous 4NP model reaction. By incorporating variably substituted ANPs into the substrate scope and averaging performance, the resulting rank of catalyst activity more accurately reflects activity trends when applied to other reducible functionalities, such as -N=N- groups in azo dyes.
Nueleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase
Ziebart, Kristin T.,Toney, Michael D.
, p. 2851 - 2859 (2010)
Anthranilate synthase (AS), aminodeoxychorismate synthase (ADCS), isochorismate synthase (IS), and salicylate synthase (SS) are structurally homologous chorismate-utilizing enzymes that carry out the first committed step in the formation of tryptophan, fo
Conversion of Anthranilate Synthase into Isochorismate Synthase: Implications for the Evolution of Chorismate-Utilizing Enzymes
Plach, Maximilian G.,L?ffler, Patrick,Merkl, Rainer,Sterner, Reinhard
, p. 11270 - 11274 (2015)
Chorismate-utilizing enzymes play a vital role in the biosynthesis of metabolites in plants as well as free-living and infectious microorganisms. Among these enzymes are the homologous primary metabolic anthranilate synthase (AS) and secondary metabolic i
Inhibition of chorismate-utilising enzymes by 2-amino-4-carboxypyridine and 4-carboxypyridone and 5-carboxypyridone analogues
Payne, Richard J.,Bulloch, Esther M. M.,Kerbarh, Olivier,Abell, Chris
, p. 3534 - 3542 (2010)
Several 2-amino-4-carboxypyridine, 4- and 5-carboxypyridone-based compounds were prepared and tested against three members of the chorismate-utilising enzyme family, anthranilate synthase, isochorismate synthase and salicylate synthase. Most compounds exhibited low micromolar inhibition of these three enzymes. The most potent inhibitor was a 4-carboxypyridone analogue bearing a lactate side chain on the pyridyl nitrogen which exhibited inhibition constants of 5, 91 and 54 μM against anthranilate synthase, isochorismate synthase and salicylate synthase respectively. The Royal Society of Chemistry 2010.
