- Investigating the ruthenium metalation of proteins: X-ray structure and Raman microspectroscopy of the complex between RNase A and AziRu.
Investigating the ruthenium metalation of proteins: X-ray structure and Raman microspectroscopy of the complex between RNase A and AziRu.
Inorganic chemistry (2013-10-08)
Alessandro Vergara, Irene Russo Krauss, Daniela Montesarchio, Luigi Paduano, Antonello Merlino
PMID24093479
ABSTRACT
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.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Ribonuclease B from bovine pancreas, BioReagent, ≥50 Kunitz units/mg protein, ≥80% (SDS-PAGE)
Sigma-Aldrich
Ribonuclease A from bovine pancreas, for molecular biology, ≥70 Kunitz units/mg protein, lyophilized
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type II-A, ≥60% (SDS-PAGE), >= 60 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, (Solution of 50% glycerol, 10mM Tris-HCL pH 8.0)
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type X-A, ≥90% (SDS-PAGE), ≥70 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein