Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications

被引:208
|
作者
Alayash, AI
Patel, RP
Cashon, RE
机构
[1] US FDA, CBER, Bethesda, MD 20892 USA
[2] Univ Alabama, Ctr Free Rad Biol, Birmingham, AL 35294 USA
[3] Univ Maine, Dept Biochem Microbiol & Mol Biol, Orono, ME 04469 USA
[4] Univ Alabama, Dept Pathol, Birmingham, AL 35294 USA
关键词
D O I
10.1089/152308601300185250
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Direct cytotoxic effects associated with hemoglobin (Hb) or myoglobin (Mb) have been ascribed to redox reactions (involving either one- or two-electron steps) between the heme group and peroxides. These interactions are the basis of the pseudoperoxidase activity of these hemoproteins and can be cytotoxic when reactive species are formed at relatively high concentrations during inflammation and typically lead to cell death. Peroxides relevant to biological systems include hydrogen peroxide, lipid hydroperoxides, and peroxynitrite. Reactions between Hb/Mb and peroxides form the ferryl oxidation state of the protein, analogous to compounds I and II formed in the catalytic cycle of many peroxidase enzymes. This higher oxidation state of the protein is a potent oxidant capable of promoting oxidative damage to most classes of biological molecules. Free iron, released from Hb, also has the potential to promote oxidative damage via classical "Fenton" chemistry. It has become increasingly evident that Hb/Mb redox reactions or their by-products play a critical role in the pathophysiology of some disease states. This review briefly discusses the reactions of Hb/Mb with biological peroxides, potential cytotoxicity and the impact of these interactions on modulation of cell signaling pathways regulated by these reactive species. Also discussed in this article is the role of heme-protein chemistry in relation to the toxicity of hemoproteins.
引用
收藏
页码:313 / 327
页数:15
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