The X-ray crystal structure of an adduct of cisplatin and bovine erythrocyte superoxide dismutase has been solved at 1.8-Å resolution. Selective platination of His19 occurs far away from the copper–zinc site. Remarkably, the protein-bound platinum center retains both chloro ligands.
Calderone, V., Casini, A., Mangani, S., Messori, L., Orioli, P.L. (2006). Structural Investigation of Cisplatin-Protein Interactions: Selective Platination of His19 in a Cuprozinc Superoxide Dismutase. ANGEWANDTE CHEMIE. INTERNATIONAL EDITION, 45(8), 1267-1269 [10.1002/anie.200502599].
Structural Investigation of Cisplatin-Protein Interactions: Selective Platination of His19 in a Cuprozinc Superoxide Dismutase
MANGANI S.;
2006-01-01
Abstract
The X-ray crystal structure of an adduct of cisplatin and bovine erythrocyte superoxide dismutase has been solved at 1.8-Å resolution. Selective platination of His19 occurs far away from the copper–zinc site. Remarkably, the protein-bound platinum center retains both chloro ligands.File | Dimensione | Formato | |
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https://hdl.handle.net/11365/2670
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