Unusual Structural Features in the Lysozyme Derivative of the Tetrakis(acetato)chloridodiruthenium(II,III) Complex

Author(s)

Messori, Luigi ^[1] ; Marzo, Tiziano ^[1] ; Fernandes Sanches, Rute Nazare ^[2] ; Hanif-Ur-Rehman ^[2] ; Silva, Denise de Oliveira ^[2] ; Merlino, Antonello ^[3]

Affiliation

^[1] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, FI - Italy

^[2] Univ Sao Paulo, Inst Quim, Dept Quim Fundamental, BR-05508000 Sao Paulo - Brazil

^[3] Univ Naples Federico II, Dept Chem Sci, I-80126 Naples - Italy

• Document type: Journal article
• Source: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION; v. 53, n. 24, p. 6172-6175, JUN 2014.
• Web of Science Citations: 25

Abstract

The reaction between the paddle-wheel tetrakis(acetato)chloridodiruthenium(II,III) complex, {[}Ru-2(mu-O2CCH3)(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 angstrom 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. (AU)

• FAPESP's process: 11/06592-1 - Anti-inflammatory and antitumor metallotherapeutic drugs: reactivity, properties and interactions with biocompatible hosts
• Grantee: Denise de Oliveira Silva
• Support Opportunities: Regular Research Grants