金属离子和环沉积肽配合物中的配体构象和金属配位异构体。

IF 3.1 2区 化学 Q2 BIOCHEMICAL RESEARCH METHODS
Emmanuel Nkyaagye, Hernando J Olivos, Thanh D Do
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引用次数: 0

摘要

极性环境中金属配合物结构表征的一个关键挑战是在低阶和高阶组装的集合中区分瞬态结构异构体。这些结构变化是由配体结构和金属配位化学的细微变化引起的,这些变化通常很难解卷积。在这里,我们利用漂管和循环离子迁移谱-质谱(IMS-MS)中的离子激活来解析已知具有选择性金属离子传输的环沉积肽配体的金属夹层配合物中的配体构象异构和金属配位异构。我们的方法揭示了由配体结构重排驱动的同分异构表现出低能量势垒,允许它们的相互转化在IMS-MS时间尺度上被捕获。相比之下,具有不同金属配位态的异构体具有较高的能量势垒,阻碍了快速的相互转化。这些发现建立了同分异构体分布与选择性金属结合和运输之间的直接关联,为环沉积肽的生物学功能提供了机制见解。这项工作强调了IMS-MS在生物学相关金属肽配体系统中解开复杂结构动力学的效用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Ligand Conformational and Metal Coordination Isomers in Complexes of Metal Ions and Cyclic Depsipeptides.

A critical challenge in the structural characterization of metal complexes in apolar environments is distinguishing transient structural isomers within an ensemble of lower- and higher-order assemblies. These structural variations arise from subtle changes in ligand architecture and metal coordination chemistry, which are often difficult to deconvolute. Here, we utilize ion activation in both drift-tube and cyclic ion mobility spectrometry-mass spectrometry (IMS-MS) to resolve ligand conformational isomerism and metal coordination isomerism in metal sandwich complexes of cyclic depsipeptide ligands known for selective metal ion transport. Our approach reveals that isomerism driven by ligand structural rearrangements exhibits low energy barriers, allowing their interconversion to be captured on the IMS-MS time scale. In contrast, isomers involving distinct metal coordination states are characterized by higher energy barriers, precluding rapid interconversion. These findings establish a direct correlation between isomer distributions and selective metal binding and transport, providing mechanistic insights into the biological functions of cyclic depsipeptides. This work underscores the utility of IMS-MS for disentangling complex structural dynamics in biologically relevant metal-peptide ligand systems.

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来源期刊
CiteScore
5.50
自引率
9.40%
发文量
257
审稿时长
1 months
期刊介绍: The Journal of the American Society for Mass Spectrometry presents research papers covering all aspects of mass spectrometry, incorporating coverage of fields of scientific inquiry in which mass spectrometry can play a role. Comprehensive in scope, the journal publishes papers on both fundamentals and applications of mass spectrometry. Fundamental subjects include instrumentation principles, design, and demonstration, structures and chemical properties of gas-phase ions, studies of thermodynamic properties, ion spectroscopy, chemical kinetics, mechanisms of ionization, theories of ion fragmentation, cluster ions, and potential energy surfaces. In addition to full papers, the journal offers Communications, Application Notes, and Accounts and Perspectives
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