Department of Chemistry, Bryn Mawr College, Bryn Mawr, PA 19010, USA.
Department of Chemistry and Chemical Biology, The University of New Mexico, Albuquerque, NM 87131, USA.
Molecules. 2023 Nov 7;28(22):7456. doi: 10.3390/molecules28227456.
The pyranopterin dithiolene ligand is remarkable in terms of its geometric and electronic structure and is uniquely found in mononuclear molybdenum and tungsten enzymes. The pyranopterin dithiolene is found coordinated to the metal ion, deeply buried within the protein, and non-covalently attached to the protein via an extensive hydrogen bonding network that is enzyme-specific. However, the function of pyranopterin dithiolene in enzymatic catalysis has been difficult to determine. This focused account aims to provide an overview of what has been learned from the study of pyranopterin dithiolene model complexes of molybdenum and how these results relate to the enzyme systems. This work begins with a summary of what is known about the pyranopterin dithiolene ligand in the enzymes. We then introduce the development of inorganic small molecule complexes that model aspects of a coordinated pyranopterin dithiolene and discuss the results of detailed physical studies of the models by electronic absorption, resonance Raman, X-ray absorption and NMR spectroscopies, cyclic voltammetry, X-ray crystallography, and chemical reactivity.
蝶啶二硫醇配体在几何和电子结构方面非常显著，仅存在于单核钼和钨酶中。蝶啶二硫醇与金属离子配位，深埋在蛋白质内，并通过广泛的氢键网络与蛋白质非共价结合，该网络具有酶特异性。然而，蝶啶二硫醇在酶催化中的功能一直难以确定。本综述旨在概述从钼的蝶啶二硫醇模型配合物研究中获得的知识，以及这些结果与酶系统的关系。这项工作首先总结了酶中蝶啶二硫醇配体的已知情况。然后，我们介绍了模拟配位蝶啶二硫醇的无机小分子配合物的发展，并讨论了通过电子吸收、共振拉曼、X 射线吸收和 NMR 光谱学、循环伏安法、X 射线晶体学和化学反应性对模型进行详细物理研究的结果。
