Unusual Structural Features in the Lysozyme Derivative of the Tetrakis(acetato)chloridodiruthenium(II,III) Complex |
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| Authors: | Prof Luigi Messori Tiziano Marzo Rute Nazaré Fernandes Sanches Hanif‐Ur‐Rehman Prof Denise de?Oliveira Silva Dr Antonello Merlino |
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| Institution: | 1. Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino (FI) (Italy);2. Departamento de Química Fundamental, Instituto de Química, Universidade de S?o Paulo, Av. Prof. Lineu Prestes, 748, B2T, 05508‐000, S?o Paulo, SP (Brazil);3. Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, Via cintia, 80126 Napoli (Italy) |
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| Abstract: | The reaction between the paddle‐wheel tetrakis(acetato)chloridodiruthenium(II,III) complex, Ru2(μ‐O2CCH3)4Cl] 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 Å 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. |
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| Keywords: | bioinorganic chemistry metallodrugs protein– metal adducts ruthenium X‐ray diffraction |
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