Cobalt-zinc carbides embedded in N-doped porous carbon nanospheres as polysulfide mediators for efficient lithium-sulfur batteries.

Developing high-efficiency interlayer catalysts is a promising tactic for improving the cycling performance of rechargeable lithium-sulfur (Li-S) batteries. Herein, using the Prussian blue analogue as the precursor, cobalt-zinc carbide nanocrystal-embedded N-doped porous carbon (Co3ZnC@NC) is synthesized via simple post-carbonization. The obtained Co3ZnC@NC nanospheres exhibit a robust core-shell structure showing good conductivity, high porosity and available metal active sites, favoring the interfacial charge transfer and the electron transport upon electrochemical reactions. The results demonstrate that the Co3ZnC@NC catalyst is quite suitable for boosting the adsorption and redox conversion kinetics of soluble polysulfides. When acting as the separator interlayer, Co3ZnC@NC contributes to improved Li-S batteries with a high discharge specific capacity of 1659.8 mA h g-1 at 0.1C and superior cycling stability of over 250 cycles at 1.0C (high capacity retention of 84.1% after 100 cycles at 0.5C). Furthermore, the Co3ZnC@NC-based battery can maintain a high discharge capacity of 734.0 mA h g-1 at 5.0C, along with delivering a stable reversible capacity of 805.4 mA h g-1 (∼5 mA h cm-2) after 50 cycles even under a high sulfur loading of 6.2 mg cm-2. This study affords a viable way to construct highly dispersed bimetal/carbon composites for efficient catalysts and renewable energy devices.

Strain-Amplified Exciton Chirality in Organic-Inorganic Hybrid Materials.

Chiral organic-inorganic hybrids combining chirality of organic molecules and semiconducting properties of inorganic frameworks generate chiral excitons without external spin injection, creating the potential for chiroptoelectronics. However, the relationship between molecular chirality and exciton chirality is still unclear. Here we show the strain-amplified exciton chirality in one-dimensional chiral metal halides. Utilizing chirality-induced spin-orbital coupling theory, we quantitatively demonstrate the impact of the strain-engineered molecular assembly of chiral cations on exciton chirality, offering a feasible way to amplify exciton chirality by molecular manipulation.

Reduced peptidoglycan synthesis capacity impairs growth of E. coli at high salt concentration.

Gram-negative bacteria have a thin peptidoglycan layer between the cytoplasmic and outer membranes protecting the cell from osmotic challenges. Hydrolases of this structure are needed to cleave bonds to allow the newly synthesized peptidoglycan strands to be inserted by synthases. These enzymes need to be tightly regulated and their activities coordinated to prevent cell lysis. To better understand this process in Escherichia coli, we probed the genetic interactions of mrcA (encodes PBP1A) and mrcB (encodes PBP1B) with genes encoding peptidoglycan amidases and endopeptidases in envelope stress conditions. Our extensive genetic interaction network analysis revealed relatively few combinations of hydrolase gene deletions with reduced fitness in the absence of PBP1A or PBP1B, showing that none of the amidases or endopeptidases is strictly required for the functioning of one of the class A PBPs. This illustrates the robustness of the peptidoglycan growth mechanism. However, we discovered that the fitness of ∆mrcB cells is significantly reduced under high salt stress and in vitro activity assays suggest that this phenotype is caused by a reduced peptidoglycan synthesis activity of PBP1A at high salt concentration.IMPORTANCEEscherichia coli and many other bacteria have a surprisingly high number of peptidoglycan hydrolases. These enzymes function in concert with synthases to facilitate the expansion of the peptidoglycan sacculus under a range of growth and stress conditions. The synthases PBP1A and PBP1B both contribute to peptidoglycan expansion during cell division and growth. Our genetic interaction analysis revealed that these two penicillin-binding proteins (PBPs) do not need specific amidases, endopeptidases, or lytic transglycosylases for function. We show that PBP1A and PBP1B do not work equally well when cells encounter high salt stress and demonstrate that PBP1A alone cannot provide sufficient PG synthesis activity under this condition. These results show how the two class A PBPs and peptidoglycan hydrolases govern cell envelope integrity in E. coli in response to environmental challenges and particularly highlight the importance of PBP1B in maintaining cell fitness under high salt conditions.

The lipoprotein DolP affects cell separation in Escherichia coli, but not as an upstream regulator of NlpD.

Bacterial amidases are essential to split the shared envelope of adjunct daughter cells to allow cell separation. Their activity needs to be precisely controlled to prevent cell lysis. In Escherichia coli, amidase activity is controlled by three regulatory proteins NlpD, EnvC and ActS. However, recent studies linked the outer membrane lipoprotein DolP (formerly YraP) as a potential upstream regulator of NlpD. In this study we explored this link in further detail. To our surprise DolP did not modulate amidase activity in vitro and was unable to interact with NlpD in pull-down and MST (MicroScale Thermophoresis) assays. Next, we excluded the hypothesis that ΔdolP phenocopied ΔnlpD in a range of envelope stresses. However, morphological analysis of double deletion mutants of amidases (AmiA, AmiB AmiC) and amidase regulators with dolP revealed that ΔamiAΔdolP and ΔenvCΔdolP mutants display longer chain length compared to their parental strains indicating a role for DolP in cell division. Overall, we present evidence that DolP does not affect NlpD function in vitro, implying that DolP is not an upstream regulator of NlpD. However, DolP may impact daughter cell separation by interacting directly with AmiA or AmiC, or by a yet undiscovered mechanism.