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 journalArticle

121 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

Fingerprint

Carbon Monoxide
Muramidase
Carbon monoxide
Enzymes
Crystal structure
Proteins
Molecules
X ray crystallography
Liquid chromatography
Inductively coupled plasma
Mass spectrometry
Infrared spectroscopy
Ligands
Crystals
Egg White
Ions
X Ray Crystallography
Liquid Chromatography
Chlorides
Mass Spectrometry

Cite this

@article{36f8c787839d4d4b8ce179d3cb23c3a1,
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{\cc}alo J L} and Romao, {Carlos Jose} and Rom{\~a}o, {Maria Jo{\~a}o}",
year = "2011",
month = "1",
day = "4",
doi = "10.1021/ja108820s",
language = "English",
volume = "133",
pages = "1192--1195",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "AMER CHEMICAL SOC",
number = "5",

}

CORM-3 Reactivity toward Proteins: The Crystal Structure of a Ru(II) Dicarbonyl-Lysozyme Complex. / Santos-silva, Teresa Sacadura; Mukhopadhyay, Abhik; Seixas, João D.; Bernardes, Gonçalo J L; Romao, Carlos Jose; Romão, Maria João.

In: Journal of the American Chemical Society, Vol. 133, No. 5, 04.01.2011, p. 1192-1195.

Research output: Contribution to journalArticle

TY - JOUR

T1 - CORM-3 Reactivity toward Proteins: The Crystal Structure of a Ru(II) Dicarbonyl-Lysozyme Complex

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

Y1 - 2011/1/4

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.

KW - METAL-CARBONYLS

KW - MONOXIDE-RELEASING MOLECULES

KW - CARBON-MONOXIDE

KW - CHEMISTRY

KW - PHARMACEUTICALS

U2 - 10.1021/ja108820s

DO - 10.1021/ja108820s

M3 - Article

VL - 133

SP - 1192

EP - 1195

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 5

ER -