了解聚和辅助因子模型复合体中的结合和结构
Yinan Li1,2, Kenny K Y Lun2, Justin Kai-Chi Lau3,4
1Center for Mass Spectrometry Research and Clinical Application, Shandong Public Health Clinical Center Affiliated to Shandong University, 46 Lishan Road, Shandong, Jinan 250012, China.
ACS physical chemistry Au
|September 29, 2025
概括
金属--化合物复合体表现出多样化的结构. 它们的化学结构由酸原理和硬/软的易斯酸/基概念来解释,揭示了可预测的结合途径.
科学领域:
- 生物有机化学 生物有机化学
- 协调化学 协调化学
- 化学物理 化学物理
背景情况:
- 金属蛋白具有多样化的结构和化学成分,这是由于金属辅因子和多功能组之间的竞争性结合.
- 了解这些相互作用对于破译金属蛋白功能和设计新的基于金属的治疗方法至关重要.
研究的目的:
- 为了研究模型[金属 - 辅助 - ]复合体中的竞争性结合.
- 使用各种分析技术,阐明这些复杂物体的结构多样性和碎片化机制.
主要方法:
- 用辅助配体 (terpy, salen) 和 (氨酸-氨酸 (RY),氨酸-氨酸-糖氨酸 (RYG)) 合成和表征金属复合物.
- 配对质谱学 (MS/MS) 有或没有衍生/替代.
- 密度函数理论 (DFT) 的计算.
- 红外多光子解离 (IRMPD) 光谱学.红外多光子解离.
主要成果:
- 复杂解离产生了丰富的基 ([RY]•+和[RYG]•+) 结构取决于金属复合物的组成.
- DFT计算提供了有关绑定模式和碎片化机制的见解.
- IRMPD光谱学证实了[Cu-(terpy) -RYG]2+的碳酸盐结合,DFT显示易于转化为与酸盐结合的结构.
结论:
- 复杂的化学,尽管其明显的复杂性,可以使用基本的酸化学和硬/软的易斯酸/ (HSLAB) 原则合理化.
- 实验和计算结果一致,支持这些化学概念的预测能力.
- 涉及多个功能组的能量最小化途径驱动了这些金属复合体中观察到的丰富的结构多样性.
相关概念视频
Cooperative Allosteric Transitions
8.6K
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...
8.6K
Cooperative Allosteric Transitions
2.6K
2.6K
Protein-protein Interfaces
14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Protein Complex Assembly
16.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.6K
Protein Complex Assembly
2.5K
2.5K
Protein and Protein Structure
86.9K
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...
86.9K


