Abstract
Peroxynitrite, a biological toxin produced in vivo by the nearly diffusion-controlled reaction of nitrogen monoxide with superoxide, can nitrate and oxidize various biomolecules. Modifications caused by peroxynitrite have been linked to many human diseases, in particular, increased levels of free or protein-bound 3-nitrotyrosine, a biomarker for peroxynitrite in vivo, have been detected in a variety of pulmonary and cardiovascular diseases as well as in neurodegenerative and chronic inflammatory disorders. These observations have led to the search for a drug that can scavenge this powerful nitrating and oxidizing agent. Heme proteins, in particular myoglobin and hemoglobin, present in large amounts in muscles and red blood cells, respectively, have been proposed to serve as sinks for peroxynitrite in these cells. This report reviews the current knowledge of the reactions of different forms of myoglobin and hemoglobin with peroxynitrite and discusses their physiological role on the basis of measured rate constants.Key words: myoglobin, hemoglobin, peroxynitrite, tyrosine nitration, iron(III) peroxynitrite complex.
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