Developing efficient,stable,and low-cost electrocatalysts toward alkaline hydrogen evolution reactions(HER)in water electrolysis driven by renewable energy sources has always been discussed over the past decade.To red...Developing efficient,stable,and low-cost electrocatalysts toward alkaline hydrogen evolution reactions(HER)in water electrolysis driven by renewable energy sources has always been discussed over the past decade.To reduce energy consumption and improve energy utilization efficiency,highly active electrocatalytic electrodes are essential for lowering the energy barrier of the HER.Catalysts featuring multiple interfaces have attracted significant research interest recently due to their enhanced physicochemical properties.Reasonable interface modulation can optimize intermediate active species’adsorption energy,improve catalytic active sites’selectivity,and enhance intrinsic catalytic activity.Here,we provided an overview of the latest advancement in interface engineering for efficient HER catalysts.We begin with a brief introduction to the fundamental concepts and mechanisms of alkaline HER.Then,we analyze and discuss current regulating principles in interface engineering for HER catalysts,focusing particularly on optimizing electron structures and modulating microenvironment reactions.Finally,the challenges and further prospects of interface catalysts for future applications are discussed.展开更多
The characterization of senescence-associated endopeptidase (EP) isoenzymes in wheat (Triticum aestivum L. cv. Yangmai 158) leaves during dark-induced senescence was performed. It was found that there was much higher ...The characterization of senescence-associated endopeptidase (EP) isoenzymes in wheat (Triticum aestivum L. cv. Yangmai 158) leaves during dark-induced senescence was performed. It was found that there was much higher endoproteolytic activity in dark-induced wheat leaves than in control. Six endopeptidase isoenzymes (EP1-EP6) were identified by natural gradient-polyacrylamide gel electrophoresis (PAGE) co-polymerized gelatin in the gel, five of which (EP1, EP2, EP4, EP5 and EP6) were only detected in senescing leaves. Treatment with 6-benzyl aminopurine (6-BA) delayed the expression of these EP isoenzymes and abscisic acid (ABA) accelerated it. The activity of EP3 could be detected at a wider range of pH and temperature levels while EP4, EP5 and EP 6 could be only detected at pH 4-5 and 30 -45 degreesC, EP1 and EP2 at pH 3-5 and 30-45 degreesC. All of the EP isoenzymes showed high thermal stability, especially EP3, EP5 and EP6 which still had activitiy even by incubation at 55 degreesC for 1 h. By using different class-specific inhibitors, EP1 and EP2 were characterized as metal-dependent cysteine-proteases, EP4 as a serine-protease.展开更多
文摘Developing efficient,stable,and low-cost electrocatalysts toward alkaline hydrogen evolution reactions(HER)in water electrolysis driven by renewable energy sources has always been discussed over the past decade.To reduce energy consumption and improve energy utilization efficiency,highly active electrocatalytic electrodes are essential for lowering the energy barrier of the HER.Catalysts featuring multiple interfaces have attracted significant research interest recently due to their enhanced physicochemical properties.Reasonable interface modulation can optimize intermediate active species’adsorption energy,improve catalytic active sites’selectivity,and enhance intrinsic catalytic activity.Here,we provided an overview of the latest advancement in interface engineering for efficient HER catalysts.We begin with a brief introduction to the fundamental concepts and mechanisms of alkaline HER.Then,we analyze and discuss current regulating principles in interface engineering for HER catalysts,focusing particularly on optimizing electron structures and modulating microenvironment reactions.Finally,the challenges and further prospects of interface catalysts for future applications are discussed.
文摘The characterization of senescence-associated endopeptidase (EP) isoenzymes in wheat (Triticum aestivum L. cv. Yangmai 158) leaves during dark-induced senescence was performed. It was found that there was much higher endoproteolytic activity in dark-induced wheat leaves than in control. Six endopeptidase isoenzymes (EP1-EP6) were identified by natural gradient-polyacrylamide gel electrophoresis (PAGE) co-polymerized gelatin in the gel, five of which (EP1, EP2, EP4, EP5 and EP6) were only detected in senescing leaves. Treatment with 6-benzyl aminopurine (6-BA) delayed the expression of these EP isoenzymes and abscisic acid (ABA) accelerated it. The activity of EP3 could be detected at a wider range of pH and temperature levels while EP4, EP5 and EP 6 could be only detected at pH 4-5 and 30 -45 degreesC, EP1 and EP2 at pH 3-5 and 30-45 degreesC. All of the EP isoenzymes showed high thermal stability, especially EP3, EP5 and EP6 which still had activitiy even by incubation at 55 degreesC for 1 h. By using different class-specific inhibitors, EP1 and EP2 were characterized as metal-dependent cysteine-proteases, EP4 as a serine-protease.
