通过活跃部位的动态结构调节,打破氧气演变中的线性缩放关系
Zheye Zhang1, Hongyan Zhao2, Shibo Xi3
1School of Chemistry, Chemical Engineering and Biotechnology, Nanyang Technological University, Singapore, Singapore.
Nature communications
|February 3, 2025
概括
研究人员通过动态调节氧气演化反应中的活性位点来规避催化剂性能限制. 这种分子催化剂设计破坏了固有的缩放关系,以改善多步骤催化.
科学领域:
- 催化剂是一种催化剂.
- 电化学 电化学 电化学
- 材料科学 材料科学 材料科学
背景情况:
- 反应性中间体的吸附能量之间的通用线性缩放关系限制了多步反应中的催化剂性能.
- 氧进化反应 (OER) 对许多能量转换技术至关重要,但受到这些扩展限制的阻碍.
研究的目的:
- 为了规避电化学氧气演化反应中的线性缩放关系.
- 开发一种具有动态活性位点调节的分子催化剂,以增强OER活动.
主要方法:
- 通过现场电化学激活构建一个模型Ni-Fe2分子催化剂.
- 利用理论计算和电动力学研究来分析催化机制.
- 研究由分子内质子转移驱动的活性位点的动态结构调节.
主要成果:
- Ni-Fe2分子催化剂表现出显著的内在氧气演化反应活性.
- 尼-酸协调的动态演变改变了Fe活性中心的电子结构.
- 同时降低了O-H和O-O债券形成的自由能量变化.
结论:
- 该研究成功地通过动态的双站合作来破坏了OER固有的扩展关系.
- 这项工作推进了分子水氧化催化剂,并为多介质催化提供了一个新的范式.
- 动态结构调节提供了一种克服催化性能局限性的策略.
相关概念视频
Cooperative Allosteric Transitions
7.8K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.8K
Allosteric Regulation
57.5K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
57.5K
Redox Equilibria: Overview
513
A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
513
Protein and Protein Structure
78.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
78.0K
Oxygen Transport in the Blood
2.4K
Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
2.4K
Multi-Step Reactions
7.2K
Chemical reactions often occur in a stepwise fashion involving two or more distinct reactions taking place in a sequence. A balanced equation indicates the reacting species and the product species, but it reveals no details about how the reaction occurs at the molecular level. The reaction mechanism (or reaction path) provides details regarding the precise, step-by-step process by which a reaction occurs. Each of the steps in a reaction mechanism is called an elementary reaction. These...
7.2K


