Metalloproteins are essential to numerous reactions in nature, and constitute approximately one-third of all known proteins. Molecular dynamics of proteins has been elucidated with great success both by experimental and theoretical methods, revealing atomic level details of function involving the organic constituents on a broad spectrum of time scales. However, the characterization of dynamics at biomolecular metal sites on nanosecond time scales is scarce in the literature. The aqua ions of many biologically relevant metal ions exhibit exchange of water molecules on the nanosecond time scale or faster, often defining their reactivity in aqueous solution, and this is presumably also a relevant time scale for the making and breaking of coordination bonds between metal ions and ligands at protein metal sites. Ligand exchange dynamics is critical for a variety of elementary steps of reactions in metallobiochemistry, for example, association and dissociation of metal bound water, association of substrate and dissociation of product in the catalytic cycle of metalloenzymes, at regulatory metal sites which require binding and dissociation of metal ions, as well as in the transport of metal ions across cell membranes or between proteins involved in metal ion homeostasis.

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蛋白质金属位点的纳秒动力学：γ射线光谱的扰动角相关（PAC）的应用

金属蛋白对于自然界中的众多反应必不可少，并构成所有已知蛋白的约三分之一。已经通过实验和理论方法阐明了蛋白质的分子动力学，并获得了巨大的成功，揭示了在广泛的时标上涉及有机成分的功能的原子级细节。然而，在文献中缺乏纳秒级时标上生物分子金属位点动力学的表征。许多生物学上相关的金属离子的水离子在纳秒级或更短的时间尺度上表现出水分子交换，通常定义了它们在水溶液中的反应性，这大概也是在金属离子之间建立和破坏配位键的相关时间尺度。和蛋白质金属位点的配体。