在亚2纳米高度稳定的活动现场集体的定向构造,以增强催化活性和选择性
Zemin Chen1, Yu Chen2, Lei Shi3
1Key Laboratory of Precision and Intelligent Chemistry, University of Science and Technology of China, Hefei, 230026, China.
Advanced materials (Deerfield Beach, Fla.)
|July 14, 2024
概括
研究人员开发了一种新策略,用于创建超小的非贵金属化物集群 (<2 nm),以提高选择性化的稳定性和催化活性. 这种方法优化了单原子和集群协同作用的网站,显著提高了性能.
科学领域:
- 材料科学 材料科学 材料科学
- 催化剂是一种催化剂.
- 纳米技术纳米技术
背景情况:
- 控制亚纳米级非贵金属催化剂的活动选择性权衡仍然是一个重大挑战.
- 开发具有高稳定性和精确设计的活性点的催化剂对于优化化学反应至关重要.
研究的目的:
- 开发一种用于构建具有增强稳定性和催化性能的2nm以下金属化物集群的新策略.
- 在选择性化中研究不同单原子和集群协同作用场所的结构-活性关系.
主要方法:
- 采用"多原子诱导的SMSI + in situ P激活"策略来合成2nm以下的金属化物集群.
- 这项研究涉及创建和表征各种亚-2nm站点,包括单原子 (Ni1),Ni1+金属集群 (Ni1+Ni_n) 和Ni1+金属化物集群 (Ni1+Ni2P_n) 协同作用的站点.
- 进行了先进的结构和机制研究,以了解催化行为.
主要成果:
- 最小的金属化物集群 (<2 nm) 通过无元至三元非贵金属系统合成,表现出前所未有的热稳定性.
- 确定了一个新的Ni1+Ni2P_n协同位点,通过协同强金属支相互作用 (SMSI) 和位点合,证明了自我优化电子结构.
- 这一Ni1+Ni2P_n位点在温和条件下,与Ni1位点相比,对基的半化催化活性增加了56倍.
结论:
- 开发的策略有效地为选择性化创建了高度稳定的2nm以下金属化物位点.
- 由于优化电子结构和动力学,Ni1+Ni2P_n协同场所显示出卓越的催化性能.
- 这项工作代表了原子利用,热稳定性和非贵金属催化剂的催化效率的重大进步.
相关概念视频
Introduction to Mechanisms of Enzyme Catalysis
8.1K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
8.1K
Enzymes
81.4K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
81.4K
Induced-fit Model
80.7K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
80.7K
Catalytically Perfect Enzymes
4.0K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Most enzymes...
Most enzymes...
4.0K
Allosteric Proteins-ATCase
5.7K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K


