Oxidation and nitrosylation of oxyhemoglobin by S-nitrosoglutathione via nitroxyl anion. Free Radic Biol Med 2003 Dec 01;35(11):1515-26
Date
12/04/2003Pubmed ID
14642399DOI
10.1016/j.freeradbiomed.2003.08.021Scopus ID
2-s2.0-0345306150 (requires institutional sign-in at Scopus site) 18 CitationsAbstract
The reaction between low molecular weight S-nitrosothiols and hemoglobin is often used to synthesize S-nitrosohemoglobin, a form of hemoglobin suggested to be involved in the regulation of vascular oxygen delivery. However, this reaction has not been studied in detail, and several groups have reported a variable co-formation of oxidized methemoglobin (metHb) during synthesis. This study examines the mechanism of metHb formation and shows that nitrosylhemoglobin (HbNO) can also be formed. Generation of metHb and HbNO is largely dependent on the presence of protein thiol groups. We present evidence for a mechanism for the formation of metHb and HbNO involving the intermediacy of nitroxyl anion. Specifically, the reaction of nitroxyl with S-nitrosothiols to liberate nitric oxide and reduced thiol is proposed to be central to the reaction mechanism.
Author List
Spencer NY, Patel NK, Keszler A, Hogg NAuthors
Neil Hogg PhD Senior Associate Dean, Professor in the Biophysics department at Medical College of WisconsinAgnes Keszler Research Scientist I in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AnionsCopper
Cysteine
Electrodes
Electron Spin Resonance Spectroscopy
Hemoglobins
Humans
Hydrogen-Ion Concentration
Kinetics
Models, Chemical
Nitric Oxide
Nitrogen
Nitrogen Oxides
Oxygen
Oxygen Consumption
Oxyhemoglobins
S-Nitrosoglutathione
S-Nitrosothiols
Time Factors
