Unusual Structural Features in the Adduct of Dirhodium Tetraacetate with Lysozyme.

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 HEWL:it 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 tw

SUBMITTER: Loreto D 

PROVIDER: S-EPMC7867343 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature