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https://www.selleckchem.com/products/ots964.html All rights reserved.Nitrogenase is the only biological catalyst that is known to convert dinitrogen (N2) to ammonia (NH3). Nitrogenase-catalyzed NH3 formation in vivo is energetically intensive due to a series of events, including a Fe protein cycle coupled with ATP hydrolysis. Furthermore, the complexity of nitrogenase's cofactors plagues related bioelec-trodes by unstable and poor electric wiring between the cofactors and the electrode, thereby lowering the overall bioelectrocatalytic perfor-mance. We report an organic redox polymer-based electroenzymatic nitrogen fixation system using a metal-free redox polymer namely neutral red-modified poly(glycidyl methacrylate-co-methylmethacry-late-co-poly(ethyleneglycol)methacrylate) with a low redox potential of -0.58 V vs. SCE. The stable and efficient electric wiring of nitrogenase within the redox polymer matrix enables mediated bioelectrocatalysis of N3-, NO2- and N2 to NH3 catalyzed by the MoFe protein via the polymer-bound redox moieties distributed in the polymer matrix in the absence of the Fe protein. Bulk bioelectrosynthetic experiments pro-duced 209 ± 30 nmol NH3 nmol MoFe-1 h-1 from N2 reduction. 15N2 labeling experiments and NMR analysis were performed to confirm biosynthetic N2 reduction to NH3.Aim The aim of the study was to investigate the difference of the serum metabolic profile between gestational diabetes mellitus (GDM) patients and preeclampsia (PE) patients, to establish the disease differentiation model and to find characteristic metabolites, in order to provide a new idea for the occurrence, development and treatment of the disease. Methods Twenty-nine patients with GDM group and 29 PE group who were examined in Tianjin No. 3 Central Hospital from March 2018 to August 2018 were enrolled as case group, and 29 normal pregnant women were selected as control group. All the serum samples were analyzed by using the ultra-performance liquid chromatography a
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