Santos Marino F A, Pessoa João Costa
Associate Laboratory i4HB-Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.
UCIBIO-Applied Molecular Biosciences Unit, Chemistry Department, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.
Molecules. 2023 Sep 9;28(18):6538. doi: 10.3390/molecules28186538.
The structural determination and characterization of molecules, namely proteins and enzymes, is crucial to gaining a better understanding of their role in different chemical and biological processes. The continuous technical developments in the experimental and computational resources of X-ray diffraction (XRD) and, more recently, cryogenic Electron Microscopy (cryo-EM) led to an enormous growth in the number of structures deposited in the Protein Data Bank (PDB). Bioinorganic chemistry arose as a relevant discipline in biology and therapeutics, with a massive number of studies reporting the effects of metal complexes on biological systems, with vanadium complexes being one of the relevant systems addressed. In this review, we focus on the interactions of vanadium compounds (VCs) with proteins. Several types of binding are established between VCs and proteins/enzymes. Considering that the V-species that bind may differ from those initially added, the mentioned structural techniques are pivotal to clarifying the nature and variety of interactions of VCs with proteins and to proposing the mechanisms involved either in enzymatic inhibition or catalysis. As such, we provide an account of the available structural information of VCs bound to proteins obtained by both XRD and/or cryo-EM, mainly exploring the more recent structures, particularly those containing organic-based vanadium complexes.
分子（即蛋白质和酶）的结构测定与表征对于更好地理解它们在不同化学和生物过程中的作用至关重要。X射线衍射（XRD）以及最近的低温电子显微镜（cryo-EM）在实验和计算资源方面的不断技术发展，导致蛋白质数据库（PDB）中沉积的结构数量大幅增长。生物无机化学作为生物学和治疗学中的一门相关学科应运而生，大量研究报道了金属配合物对生物系统的影响，钒配合物就是其中一个被研究的相关体系。在本综述中，我们重点关注钒化合物（VCs）与蛋白质的相互作用。VCs与蛋白质/酶之间建立了几种类型的结合。考虑到结合的钒物种可能与最初添加的不同，上述结构技术对于阐明VCs与蛋白质相互作用的性质和多样性以及提出酶抑制或催化所涉及的机制至关重要。因此，我们介绍了通过XRD和/或cryo-EM获得的与蛋白质结合的VCs的现有结构信息，主要探讨了最新的结构，特别是那些含有有机基钒配合物的结构。
