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.

Protein interactions of dirhodium tetraacetate: a structural study / Ferraro G.; Pratesi A.; Messori L.; Merlino A.. - In: DALTON TRANSACTIONS. - ISSN 1477-9226. - ELETTRONICO. - 49:(2020), pp. 2412-2416. [10.1039/c9dt04819g]

Protein interactions of dirhodium tetraacetate: a structural study

Messori L.
;
Merlino A.
2020

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.
2020
49
2412
2416
Ferraro G.; Pratesi A.; Messori L.; Merlino A.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1259335
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