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Protein interactions of dirhodium tetraacetate: a structural study

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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.

Graphical abstract: Protein interactions of dirhodium tetraacetate: a structural study

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Article information


Submitted
19 Dec 2019
Accepted
28 Jan 2020
First published
28 Jan 2020

Dalton Trans., 2020, Advance Article
Article type
Communication

Protein interactions of dirhodium tetraacetate: a structural study

G. Ferraro, A. Pratesi, L. Messori and A. Merlino, Dalton Trans., 2020, Advance Article , DOI: 10.1039/C9DT04819G

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