The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects.
The interaction of ascorbate with different heme iron redox states of myoglobin (ferrylmyoglobin, FeIV = O; metmyoglobin, FeIII; and oxymyoglobin, FeIIO2) was examined by e.s.r. and absorption spectroscopy. The reaction of ascorbate with ferryl- or met-myoglobin resulted in ascorbyl radical production. The interaction of ascorbate with oxymyoglobin proceeded with formation of ascorbyl radical, hydrogen peroxide, and an overall oxidation of oxymyoglobin to metmyoglobin. The latter reaction proceeded via an oxoferryl complex intermediate-corresponding to ferrylmyoglobin and identified by treatment of the reaction mixture with Na2S. These observations are consistent with a concerted electron transfer mechanism, whereby the two electrons required for the reduction of oxygen to hydrogen peroxide are donated by ascorbic acid and the heme iron. The antioxidant and prooxidant aspects of these redox transitions are discussed in terms of their kinetic properties.
Giulivi
C
C
Department of Molecular Pharmacology and Toxicology, University of Southern California, Los Angeles 90033.
Cadenas
E
E
D000818:Animals; D000975:Antioxidants; D001205:Ascorbic Acid / Q000737:chemistry* / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D006736:Horses; D007501:Iron / Q000737:chemistry* / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D016877:Oxidants; D010084:Oxidation-Reduction; D011048:Polarography; D013053:Spectrophotometry
D000975:Antioxidants; D005609:Free Radicals; D009211:Myoglobin; D016877:Oxidants; D006418:Heme; D007501:Iron; D001205:Ascorbic Acid