Unusual Structural Features in the Adduct of Dirhodium Tetraacetate with Lysozyme.
Int J Mol Sci
; 22(3)2021 Feb 02.
Article
em En
| MEDLINE
| ID: mdl-33540880
ABSTRACT
The structures of the adducts formed upon reaction of the cytotoxic paddlewheel dirhodium complex [Rh2(µ-O2CCH3)4] with the model protein hen egg white lysozyme (HEWL) under different experimental conditions are reported. Results indicate that [Rh2(µ-O2CCH3)4] extensively reacts with HEWLit in part breaks down, at variance with what happens in reactions with other proteins. A Rh center coordinates the side chains of Arg14 and His15. Dimeric Rh-Rh units with Rh-Rh distances between 2.3 and 2.5 Å are bound to the side chains of Asp18, Asp101, Asn93, and Lys96, while a dirhodium unit with a Rh-Rh distance of 3.2-3.4 Å binds the C-terminal carboxylate and the side chain of Lys13 at the interface between two symmetry-related molecules. An additional monometallic fragment binds the side chain of Lys33. These data, which are supported by replicated structural determinations, shed light on the reactivity of dirhodium tetracarboxylates with proteins, providing useful information for the design of new Rh-containing biomaterials with an array of potential applications in the field of catalysis or of medicinal chemistry and valuable insight into the mechanism of action of these potential anticancer agents.
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Base de dados:
MEDLINE
Assunto principal:
Compostos Organometálicos
/
Muramidase
Limite:
Animals
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article