Investigating the Ruthenium Metalation of Proteins: X-ray Structure and Raman Microspectroscopy of the Complex between RNase A and AziRu(411 views) Vergara A, Russo Krauss I, Montesarchio D, Paduano L, Merlino A
Department of Chemical Sciences, University of Naples Federico II, Napoli, Italy
CNR Institute of Biostructures and Bioimages, Napoli, Italy
CSGI (Consorzio per Lo Sviluppo Dei Sistemi A Grande Interfase), Florence, Italy
References: Not available.
Investigating the Ruthenium Metalation of Proteins: X-ray Structure and Raman Microspectroscopy of the Complex between RNase A and AziRu
A Raman-assisted crystallographic study on the adduct between AziRu, a Ru(III) complex with high antiproliferative activity, and RNase A is presented. The protein structure is not perturbed significantly by the Ru label. The metal coordinates to ND atoms of His105 or of His119 imidazole rings, losing all of its original ligands but retaining octahedral, although distorted, coordination geometry. The AziRu binding inactivates the enzyme, suggesting that its antitumor action can be exerted by a mechanism of competitive inhibition.
Investigating the Ruthenium Metalation of Proteins: X-ray Structure and Raman Microspectroscopy of the Complex between RNase A and AziRu
No results.
Investigating the Ruthenium Metalation of Proteins: X-ray Structure and Raman Microspectroscopy of the Complex between RNase A and AziRu
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