7251-61-8Relevant articles and documents
Studies on methylglyoxal 1. Fluorometric determination of methylglyoxal using high-performance liquid chromatography
Matsuura,Yoshino,Ooki,et al.
, p. 3567 - 3570 (1985)
A high-performance liquid chromatographic (HPLC) method has been developed for the determination of methylglyoxal (MG). When MG was treated with o-phenylenediamine and trichloroacetic acid, it was converted to a highly fluorescent new compound, 2-(2-benzimidazolyl)-3-methylquinoxaline (BIMQ) the chemical structure of which was elucidated by NMR and MS. BIMQ was analyzed by HPLC using a 4 mm x 25 mm column packed with LiChrosorb Si-60 (10 μ). This method is highly sensitive and was satisfactorily applied to the measurement of MG in biological materials.
Bio-inspired Maillard-Like reactions enable a simple and sensitive assay for colorimetric detection of methylglyoxal
Wang, Shih-Ting,Lin, Yiyang,Spicer, Christopher D.,Stevens, Molly M.
, p. 11026 - 11029 (2015)
A simple and selective assay for detecting methylglyoxal (MGO), a metabolite associated with diabetes, was developed by combining a bio-inspired chemical reaction with the anti-aggregation of gold nanoparticles. This assay could detect MGO at as low as 1 μM by the naked eye and 0.05 μM by UV/vis spectrometry, within the clinical range marking oxidative stress in diabetes, and demonstrated high selectivity over other physiologically relevant ketones and aldehydes.
Decarboxylation of Aromatic Carboxylic Acids by the Prenylated-FMN-dependent Enzyme Phenazine-1-carboxylic Acid Decarboxylase
Datar, Prathamesh M.,Marsh, E. Neil G.
, p. 11723 - 11732 (2021/09/28)
Phenazine-1-carboxylic acid decarboxylase (PhdA) is a member of the expanding class of prenylated-FMN-dependent (prFMN) decarboxylase enzymes. These enzymes have attracted interest for their ability to catalyze (de)carboxylation reactions on aromatic rings and conjugated double bonds. Here we describe a method to reconstitute PhdA with prFMN that produces an active and stable form of the holo-enzyme that does not require prereduction with dithionite for activity. We establish that oxidized phenazine-1-carboxylate (PCA) is the substrate for decarboxylation, withkcat= 2.6 s-1andKM= 53 μM. PhdA also catalyzes the much slower exchange of solvent deuterium into the product, phenazine, with an apparent turnover number of 0.8 min-1. The enzyme was found to catalyze the decarboxylation of a broad range of polyaromatic carboxylic acids, including anthracene-1-carboxylic acid. Previously described prFMN-dependent aromatic (de)carboxylases have utilized electron-rich phenolic or heterocyclic molecules as substrates. PhdA extends the substrate range of prFMN-dependent (de)carboxylases to electron-poor and unfunctionalized aromatic systems, suggesting that it may prove a useful catalyst for the regioselective (de)carboxylation of otherwise unreactive aromatic molecules.
NaOH-Mediated Direct Synthesis of Quinoxalines from o-Nitroanilines and Alcohols via a Hydrogen-Transfer Strategy
Wang, Yan-Bing,Shi, Linlin,Zhang, Xiaojie,Fu, Lian-Rong,Hu, Weinan,Zhang, Wenjing,Zhu, Xinju,Hao, Xin-Qi,Song, Mao-Ping
, p. 947 - 958 (2021/01/14)
A NaOH-mediated sustainable synthesis of functionalized quinoxalines is disclosed via redox condensation of o-nitroamines with diols and α-hydroxy ketones. Under optimized conditions, various o-nitroamines and alcohols are well tolerated to generate the desired products in 44-99% yields without transition metals and external redox additives.
