二醋酸合二价钉的蛋白相互作用：结构研究。

Protein interactions of dirhodium tetraacetate: a structural study.

机构信息

Department of Chemistry "Ugo Schiff", University of Florence, via della Lastruccia, 3-13, 50019, Sesto Fiorentino, Florence, Italy.

Department of Chemistry and Industrial Chemistry, University of Pisa, Via Giuseppe Moruzzi 13, 56124, Pisa, Italy.

出版信息

Dalton Trans. 2020 Feb 25;49(8):2412-2416. doi: 10.1039/c9dt04819g.

DOI:10.1039/c9dt04819g

PMID:32022076

Abstract

The interactions between the cytotoxic paddlewheel dirhodium complex [Rh2(μ-O2CCH3)4] and the model protein bovine pancreatic ribonuclease (RNase A) were investigated by high-resolution mass spectrometry and X-ray crystallography. The results indicate that [Rh2(μ-O2CCH3)4] extensively reacts with RNase A. The metal compound binds the protein via coordination of the imidazole ring of a His side chain to one of its axial sites, while the dirhodium center and the acetato ligands remain unmodified. Data provide valuable information for the design of artificial dirhodium-containing metalloenzymes.

摘要

高分辨率质谱和 X 射线晶体学研究了细胞毒性桨轮二价铑配合物[Rh2(μ-O2CCH3)4]与模型蛋白牛胰腺核糖核酸酶（RNase A）之间的相互作用。结果表明，[Rh2(μ-O2CCH3)4]与 RNase A 广泛反应。该金属化合物通过组氨酸侧链的咪唑环与其中一个轴向位置配位来结合蛋白质，而二价铑中心和乙酸根配体保持不变。这些数据为设计人工含二价铑金属酶提供了有价值的信息。