4OOO
X-ray structure of the lysozyme derivative of tetrakis(acetato)chlorido diruthenium(II,III) complex
Summary for 4OOO
| Entry DOI | 10.2210/pdb4ooo/pdb |
| Related | 4OOT |
| Descriptor | Lysozyme C, CHLORIDE ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Gallus gallus (bantam,chickens) |
| Total number of polymer chains | 1 |
| Total formula weight | 15443.50 |
| Authors | Merlino, A. (deposition date: 2014-02-03, release date: 2014-06-18, Last modification date: 2024-11-20) |
| Primary citation | Messori, L.,Marzo, T.,Sanches, R.N.,Hanif-Ur-Rehman,de Oliveira Silva, D.,Merlino, A. Unusual Structural Features in the Lysozyme Derivative of the Tetrakis(acetato)chloridodiruthenium(II,III) Complex. Angew.Chem.Int.Ed.Engl., 53:6172-6175, 2014 Cited by PubMed 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. PubMed: 24796316DOI: 10.1002/anie.201403337 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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