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

doi:10.1021/ja108820s

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 journal › Article › peer-review

193 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 language	English
Pages (from-to)	1192-1195
Journal	Journal of the American Chemical Society
Volume	133
Issue number	5
DOIs	https://doi.org/10.1021/ja108820s
Publication status	Published - 4 Jan 2011

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

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.",

keywords = "METAL-CARBONYLS, MONOXIDE-RELEASING MOLECULES, CARBON-MONOXIDE, CHEMISTRY, PHARMACEUTICALS",

author = "Santos-silva, {Teresa Sacadura} and Abhik Mukhopadhyay and Seixas, {Jo{\~a}o D.} and Bernardes, {Gon{\c c}alo J L} and Romao, {Carlos Jose} and Rom{\~a}o, {Maria Jo{\~a}o}",

year = "2011",

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AU - Santos-silva, Teresa Sacadura

AU - Mukhopadhyay, Abhik

AU - Seixas, João D.

AU - Bernardes, Gonçalo J L

AU - Romao, Carlos Jose

AU - Romão, Maria João

PY - 2011/1/4

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N2 - 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.

AB - 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.

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KW - MONOXIDE-RELEASING MOLECULES

KW - CARBON-MONOXIDE

KW - CHEMISTRY

KW - PHARMACEUTICALS

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 5

ER -

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

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