Publication Abstract from PubMed
The reaction between the paddle-wheel tetrakis(acetato)chloridodiruthenium(II,III) complex, [Ru2 (mu-O2 CCH3 )4 Cl] and hen egg-white lysozyme (HEWL) was investigated through ESI-MS and UV/Vis spectroscopy and the formation of a stable metal-protein adduct was unambiguously demonstrated. Remarkably, the diruthenium core is conserved in the adduct while two of the four acetate ligands are released. The crystal structure of this diruthenium-protein derivative was subsequently solved through X-ray diffraction analysis to 2.1 A resolution. The structural data are in agreement with the solution results. It was found that HEWL binds two diruthenium moieties, at Asp101 and Asp119, respectively, with the concomitant release of two acetate ligands from each diruthenium center.
Unusual Structural Features in the Lysozyme Derivative of the Tetrakis(acetato)chloridodiruthenium(II,III) Complex.,Messori L, Marzo T, Sanches RN, Hanif-Ur-Rehman, de Oliveira Silva D, Merlino A Angew Chem Int Ed Engl. 2014 Jun 10;53(24):6172-5. doi: 10.1002/anie.201403337., Epub 2014 May 5. PMID:24796316[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
