Understanding the low temperature electrochemistry of magnesium-lithium hybrid ion battery in all-phenyl-complex solutions

Magnesium–lithium hybrid ion batteries have emerged as a new class of energy storage systems owing to dendrite free cycling of magnesium anode and possibility of practice of numerous conventional lithium cathodes. In present work, we used hybrid ion strategy to analyze the performance of lithium titanate based lithium cathode, magnesium metal anode, and all-phenyl complex (APC) electrolytes at different temperature

Uncovering electrochemistries of rechargeable magnesium-ion batteries at low and high temperatures

Rechargeable magnesium ion batteries, which possess the advantages of low cost, high safety, high volumetric capacity, and dendrite free cycling, have emerged as one of the potential contenders alleviate the burden on ex isting lithium ion battery technologies. Within this context, the electrochemical performance of Mg-ion batteries at high and ultra-low temperatures have attracted research attention due to their suitability for use in extreme environments (i.e. military and space station purposes). To meet the requirements for operation over wide tem perature ranges, extensive studies are being conducted to explore different cathodes, anodes, electrolytes, and interfacial phenomena. There is no review that compares the characteristics of magnesium ion batteries in terms of their working mechanism, current challenges, working voltages, possible cathode materials, and resultant elec trochemistry at different temperatures. To fulfil this research gap, we summarize the recent advances made in the development of magnesium ion batteries, including high-capacity cathodes, nucleophilic and non-nucleophilic electrolytes, hybrid ion tactics, working mechanisms, their high temperature and ultra-low temperature electrochemical performances. Future recommendations for the development of magnesium ion batteries with high energy densities capable of operating under extreme environmental conditions are also presented

Debating the magnesium–selenium battery technology

Magnesium ion batteries (MIBs) have received tremendous research attention owing to their low cost, dendrite free electroplating, and high theoretical capacities compared with lithium ion batteries (LIBs). Despite these advantages, the launching of MIBs is hindered by sluggish kinetics of the magnesium ions inside the host cathodes. Recently, several magnesium–selenium batteries have been developed to achieve the fast kinetics of magnesium ions inside the selenium-based cathodes. Herein, we have critically reviewed the five-year advancements made in the field of selenium cathode design, selenium loadings, compatible organic and inorganic electrolytes, their resultant reversible capacities, working voltages, cycle life, and specific energies. Selected selenium-based cathodes were critically debated in terms of their electrochemical performance and challenges. At the end of this review article, several innovative directions are proposed to shed light on future research

Schematic illustration of strategy.

<p>(<b>1</b>) Collected DYNLL1 binding motif sequences and PDBSum database was screened for these motifs. (<b>2</b>) Candidate proteins containing the DYNLL1 interaction motifs were picked (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0076730#pone-0076730-t002" target="_blank">Table 2</a>, bold hits). The selected proteins were tested by molecular docking against DYNLL1 to verify the hits which bind to DYNLL1 specific binding pocket. (<b>3</b>) Selected DYNLL1-interacting proteins on the basis of binding score values and common docking poses. (<b>4</b>) 3D structure comparison of DYNLL1 binding partners was carried out to examine the motif similarity pattern. (<b>5</b>) 3D structure comparison among known and novel DYNLL1 interacting proteins was conducted to inspect the structural conservation of putative DYNLL1 binding motifs and to evaluate the similarity of interacting mode. (<b>6</b>) Candidate proteins exhibiting highly conserved and identical binding pattern to the known one were selected. (<b>7</b>) Finally, annotated the possible pathways for the functional basis of novel interactions.</p

Roles of DYNLL1 and Pilin in host defense mechanism.

<p>Model of normal cell host defense mechanism. Pilin and flagellin trigger inflammasome activity in NLRC4 inflammasome activation pathway. DYNLL1/LC8 regulates NF-κβ activation by inhibiting the phosphorylation of Iκβα by Iκβ kinase.</p

Role of DYNLL1-Pilin interaction during chronic inflammation.

<p>Model of <i>P. aeruginosa</i> infected cell pathway. (1) DYNLL1/LC8-Pilin interaction interrupts the reduction mechanism of TRP14 by maintaining DYNLL1 in oxidized homodimeric form which is unable to bind with Iκβα. Iκβα is instantly degraded due to continuous phosphorylation by Iκβ kinase, resulting in up regulation of NF-κβ pathway. (2) Pilin hijacks DYNLL1 to obtain compartmental specificity and inflammasome activation.</p

Structural comparisons of all possible combinations of binding motifs.

<p>Individual RMSD values are plotted against the corresponding superposed motifs to all the indicated proteins including Pilin (KSTQD), Adenain (KSTQT), BimEL (KSTQT), DNMT3A (LGIQV), EML3 (RGTQT), nNOS (TGIQV), PAK1 (DVATS), Rack1 (YTVQD), P protein Mokola virus (KSTQT), P protein Rabies virus (KSTQT) and Vaccinia polymerase (KQTQT). The RMSD analysis shows that Pilin specific motif contains a close structural similarity to the validated DYNLL1 binding motifs.</p

Structural and conformational adjustments of DYNLL1-Pilin system at different time scales.

<p>Snapshots were collected throughout the MD simulations of each system and PDBs were generated for 1, 5, 10, 12 and 15-dependent behavior and stability of each system. PDB structures were visualized in UCSF Chimera 1.7.0. 2D plots were generated through DIMPLOT and residues involved hydrogen bonding (indicated by black dotted lines) were monitored. The Pilin specific residues involved in hydrogen bonding are indicated by joining pink dotted circles. The observed DYNLL1-loop measurements were 24.62 Å, 24.49 Å, 27.83 Å, 25.07 Å and 23.36 Å, respectively. The binding energy values at indicated time scales were −5384.58 kJ/mol, −5100.22 kJ/mol, −4848.70 kJ/mol, −5017.51 kJ/mol and 5003.91 kJ/mol, respectively. Superimposed structures at the indicated time intervals for DYNLL1 are indicated by pink (1 ns), cyan (5 ns), blue (10 ns), pink (12 ns) and yellow (15 ns) colors, respectively.</p

Residual contributions of DYNLL1 and Pilin explored through multiple docking protocols.

<p>The interacting residues of (A) DYNLL1 binding groove and (B) Pilin receptor binding domain are indicated. The residues marked in blue color are common among all the best docking poses, yellow and green colors indicate the residues which are common in 3 and 4 poses, respectively out of the 5 docking results. Pilin specific motif (KSTQD) is shown by black rectangle. Red rectangle highlights Lys130 residue which is only present in PAO strain. The docking/binding energy values for DYNLL1-Pilin obtained through individual docking procedures are: AUTODOCK, 0.9 kcal/mol; PatchDock, −28.31 kcal/mol; ZDOCK, −20.76 kcal/mol; DOCK/PIERR, −37.08 kcal/mol; CLUSPRO, −647.5 kcal/mol, respectively.</p

Conservation pattern of Pilin receptor binding domain.

<p>Pilin receptor binding domains (128-144 AA) of different strains of <i>P. aeruginosa </i><a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0076730#pone.0076730-Ivankov1" target="_blank">[60]</a> are indicated and aligned. The Pilin protein of PAO strain contains a putative DYNLL1 binding motif which is highlighted by red rectangle. The black and dark gray colors show motif conservation pattern among four strains of <i>P. aeruginosa</i>, respectively.</p