CORM-3 Reactivity toward Proteins: The Crystal Structure of a Ru(II) Dicarbonyl-Lysozyme Complex

Teresa Sacadura Santos-silva, Abhik Mukhopadhyay, João D. Seixas, Gonçalo J L Bernardes, Carlos Jose Romao, Maria João Romão

Research output: Contribution to journalArticlepeer-review

137 Citations (Scopus)

Abstract

CORM-3, [fac-Ru(CO)(3)Cl(kappa(2)-H2NCH2-CO2)], is a well-known carbon monoxide releasing molecule (CORM) capable of delivering CO in vivo. Herein we show for the first time that the interactions of CORM-3 with proteins result in the loss of a chloride ion, glycinate, and one CO ligand. The rapid formation of stable adducts between the protein and the remaining cis-Ru-II(CO)(2) fragments was confirmed by Inductively Coupled Plasma-Atomic Emission Spectrocopy (ICP-AES), Liquid-Chromatography Mass Spectrometry (LC-MS), Infrared Spectroscopy (IR), and X-ray crystallography. Three Ru coordination sites are observed in the structure of hen egg white lysozyme crystals soaked with CORM-3. The site with highest Ru occupancy (80%) shows a fac-[(His15)Ru(CO)(2)(H2O)(3)] structure.
Original languageEnglish
Pages (from-to)1192-1195
JournalJournal of the American Chemical Society
Volume133
Issue number5
DOIs
Publication statusPublished - 4 Jan 2011

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