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

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...

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Published in:Angewandte Chemie 2014-06, Vol.126 (24), p.6286-6289
Main Authors: Messori, Luigi, Marzo, Tiziano, Sanches, Rute Nazaré Fernandes, Hanif-Ur-Rehman, de Oliveira Silva, Denise, Merlino, Antonello
Format: Article
Language:eng ; ger
Subjects:
Acetates
Adducts
Bioanorganische Chemie
Chemistry
Crystal structure
Derivatives
Diffraction
Ligands
Lysozyme
Metallowirkstoffe
Protein-Metall-Addukte
Ruthenium
Röntgenbeugung
Spectroscopy
X-rays
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cited_by cdi_FETCH-LOGICAL-c2337-e48477067e526975bb8641d64d4e47eebaf9fc10ae13df5925cc992dfa0ba6213
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container_issue 24
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container_title Angewandte Chemie
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creator Messori, Luigi
Marzo, Tiziano
Sanches, Rute Nazaré Fernandes
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de Oliveira Silva, Denise
Merlino, Antonello
description 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. Räderwerk: Das Addukt aus dem Schaufelrad‐förmigen Tetrakis(acetato)chloridodiruthenium(II,III)‐Komplex und dem Hühnereiweißlysozym (türkisfarbenes Band) wurde mithilfe von ESI‐Massenspektrometrie und Röntgenbeugung charakterisiert. Dabei wurden ungewöhnliche und interessante Merkmale der Bindung der Dirutheniumzentren (eingekreist) an die Proteinseitenketten enthüllt.
doi_str_mv 10.1002/ange.201403337
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subjects Acetates
Adducts
Bioanorganische Chemie
Chemistry
Crystal structure
Derivatives
Diffraction
Ligands
Lysozyme
Metallowirkstoffe
Protein-Metall-Addukte
Ruthenium
Röntgenbeugung
Spectroscopy
X-rays
title Unusual Structural Features in the Lysozyme Derivative of the Tetrakis(acetato)chloridodiruthenium(II,III) Complex
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