5 research outputs found
Table1_Porous single-crystalline molybdenum nitride enhances electroreduction of nitrogen to ammonia.DOCX
The industrial ammonia synthesis reaction has the disadvantage of large energy consumption; thus, the electrochemical reduction method of ammonia synthesis characterized by its clean nature and environmental protectiveness has received extensive attention. Molybdenum nitride is a commonly used electrocatalyst for ammonia synthesis, and its Faraday efficiency is low, which may be due to many internal grain boundaries and few active sites. In this work, we grow microscale porous Mo2N single crystals and polycrystalline Mo2N from non-porous MoO3 single crystals. Porous molybdenum nitride materials facilitate charge transport in grain boundaries due to their single-crystal nature and enhance the catalytic properties of ammonia synthesis reactions. Compared with polycrystalline Mo2N, the porous Mo2N single crystal shows better performance, with a high NH4+ yield of 272.56 μg h−1 mg−1 and a Faradaic efficiency of 7.3%. In addition, the porous Mo2N single crystal exhibits superior long-term stability with little attenuation after 16 h electrolysis reaction. It provides a new method for the catalyst of ammonia synthesis.</p
Quantitative Phosphoproteome of Infant Formula: New Insights into the Difference of Phosphorylation in Milk Proteins between Bovine and Goat Species
Phosphorylation
is a broad post-translational protein modification,
and the level of phosphorylation of milk proteins is associated with
lactation, coagulation properties, and digestibility. However, phosphoproteins
in bovine milk-based and goat milk-based infant formula have not been
systematically explored. Here, we have analyzed six bovine and six
goat milk-based infant formula using a quantitative phosphoproteomics
approach, from which we identified 200 phosphoproteins with 276 phosphorylation
sites and 156 phosphorylation sites from 75 phosphoproteins, respectively.
Of these, 99 phosphorylation sites from 26 shared phosphoproteins
were differentially expressed between bovine and goat milk-based infant
formula. Especially, CSN1S1 was the most phosphoprotein with 25 quantified
phosphorylation sites. Gene Ontology (GO) and Kyoto Encyclopedia of
Genes and Genomes (KEGG) analyses showed that the identified phosphoproteins
not only provide nutrition to the infant but also have anti-inflammatory,
antipathogenic, and other biological functions. Our results shed light
on the composition, phosphorylation sites, and biological functions
of phosphoproteins in bovine milk and goat milk-based infant formula,
which provide new insights into the key role of protein modifications
during infant development. It also helps us to better understand the
differences in digestibility of infant formula from different animal
milk sources and thus guides the choice of milk source for infant
formula
Quantitative Phosphoproteome of Infant Formula: New Insights into the Difference of Phosphorylation in Milk Proteins between Bovine and Goat Species
Phosphorylation
is a broad post-translational protein modification,
and the level of phosphorylation of milk proteins is associated with
lactation, coagulation properties, and digestibility. However, phosphoproteins
in bovine milk-based and goat milk-based infant formula have not been
systematically explored. Here, we have analyzed six bovine and six
goat milk-based infant formula using a quantitative phosphoproteomics
approach, from which we identified 200 phosphoproteins with 276 phosphorylation
sites and 156 phosphorylation sites from 75 phosphoproteins, respectively.
Of these, 99 phosphorylation sites from 26 shared phosphoproteins
were differentially expressed between bovine and goat milk-based infant
formula. Especially, CSN1S1 was the most phosphoprotein with 25 quantified
phosphorylation sites. Gene Ontology (GO) and Kyoto Encyclopedia of
Genes and Genomes (KEGG) analyses showed that the identified phosphoproteins
not only provide nutrition to the infant but also have anti-inflammatory,
antipathogenic, and other biological functions. Our results shed light
on the composition, phosphorylation sites, and biological functions
of phosphoproteins in bovine milk and goat milk-based infant formula,
which provide new insights into the key role of protein modifications
during infant development. It also helps us to better understand the
differences in digestibility of infant formula from different animal
milk sources and thus guides the choice of milk source for infant
formula
Highly Efficient CO<sub>2</sub> Electrolysis on Cathodes with Exsolved Alkaline Earth Oxide Nanostructures
The solid oxide CO<sub>2</sub> electrolyzer
has the potential to
provide storage solutions for intermittent renewable energy sources
as well as to reduce greenhouse gas emissions. One of the key challenges
remains the poor adsorption and activity toward CO<sub>2</sub> reduction
on the electrolyzer cathode at typical operating conditions. Here,
we show a novel approach in tailoring a perovskite titanate (La, Sr)ÂTiO<sub>3+δ</sub> cathode surface, by the <i>in situ</i> growing
of SrO nanoislands from the host material through the control of perovskite
nonstoichiometry. These nanoislands provide very enhanced CO<sub>2</sub> adsorption and activation, with stability up to 800 °C, which
is shown to be in an intermediate form between carbonate ions and
molecular CO<sub>2</sub>. The activation of adsorbed CO<sub>2</sub> molecules results from the interaction of exsolved SrO nanoislands
and the defected titanate surface as revealed by DFT calculations.
These cathode surface modifications result in an exceptionally high
direct CO<sub>2</sub> electrolysis performance with current efficiencies
near 100%