SYNTHESIS, CHARACTERIZATION AND ADSORPTION STUDIES OF PHOSPHORYLATED CELLULOSE FOR THE RECOVERY OF LITHIUM FROM AQUEOUS SOLUTIONS

"In this study, pristine cellulose was functionalized by the phosphorylation reaction to make it suitable for lithium separation. After characterization studies of the synthesized adsorbent with SEM, EDX, FTIR, TGA and XPS, the effects of various parameters on the lithium uptake capacity of the adsorbent were examined. The analysis of equilibrium data by several adsorption models showed that maximum adsorption capacity of the adsorbent was found to be 9.60 mg/g at 25 °C by the Langmuir model. As initial concentration and contact time increased, adsorption capacity also increased, however, mild temperature (25-35 °C) and pH (5-6) were better for the adsorption of lithium. 80% of lithium adsorption within three minutes proved the fast kinetic nature of the adsorbent. A 99.5% desorption efficiency of lithium was achieved with 0.5 M H2SO4, among HCl and NaCl with different molarities. Phosphorylated cellulose was shown to be a favorable adsorbent for the recovery of lithium from aqueous solutions."

Structural basis of phosphorylation kinetics in the transcriptional activation domain (TAD) of c-Jun and insight of two new phosphorylation sites Ser58 and Thr62

Protein phosphorylation is one of the most important posttranslational modifications observed on biomolecules. Nearly one-third of the cell cycle protein undergoes phosphorylation at some stage of the lifespan. Multi-site phosphorylation is well known in biological systems, including those in transcription factors. Multisite phosphorylation on transcription factors brings about their activation and/or inactivation. c-Jun is one of such transcription factors, whose function is dependent upon the state of phosphorylation. N-terminal phosphorylation required for c-Jun activity, while C-terminal one suppresses its activity. c-Jun contains a transcriptional activation domain (TAD) at N-terminus. It is known that four residues viz., Ser63, Ser73, Thr91 and Thr93 get phosphorylated which is required for its functional dimerization. However, there is no evidence if there exists any phosphorylation kinetics in c-Jun. In this paper, for the first time, it has been demonstrated that there exist phosphorylation kinetics within TAD. NMR based analysis suggested that Ser63 follows the fast kinetic while, Thr91 slow and Ser73 and Thr93 fall in the intermediate category. The four sites follow the following trend in their kinetics Ser63 > Ser73 > Thr93 > Thr91. Similar phosphorylation kinetics was also observed inside the C3H 10T0.5 fibroblast. NMR-based experiments also suggested the phosphorylation of two additional sites at Ser58 and Thr62. However, a detailed significance of these phosphorylation kinetic, as well as newly identified sites, is yet to be discovered.

Single atom catalysts supported on N-doped graphene toward fast kinetic Li−S batteries: a theoretical study

To suppress the shuttle effect of lithium polysulfides and promote fast kinetics of charge−discharge process in Li−S batteries, it is essential to search promising catalysts with sufficient stability and high...

Probing the Proton-Loading Site of Cytochrome C Oxidase Using Time-Resolved Fourier Transform Infrared Spectroscopy

Crystal structure analyses at atomic resolution and FTIR spectroscopic studies of cytochrome c oxidase have yet not revealed protonation or deprotonation of key sites of proton transfer in a time-resolved mode. Here, a sensitive technique to detect protolytic transitions is employed. In this work, probing a proton-loading site of cytochrome c oxidase from Paracoccus denitrificans with time-resolved Fourier transform infrared spectroscopy is presented for the first time. For this purpose, variants with single-site mutations of N131V, D124N, and E278Q, the key residues in the D-channel, were studied. The reaction of mutated CcO enzymes with oxygen was monitored and analyzed. Seven infrared bands in the “fast” kinetic spectra were found based on the following three requirements: (1) they are present in the “fast” phases of N131V and D124N mutants, (2) they have reciprocal counterparts in the “slow” kinetic spectra in these mutants, and (3) they are absent in “fast” kinetic spectra of the E278Q mutant. Moreover, the double-difference spectra between the first two mutants and E278Q revealed more IR bands that may belong to the proton-loading site protolytic transitions. From these results, it is assumed that several polar residues and/or water molecule cluster(s) share a proton as a proton-loading site. This site can be propionate itself (holding only a fraction of H+), His403, and/or water cluster(s).