Abstract
Publisher Summary This chapter discusses the molecular mechanisms and methodological aspects of the reaction of two major classes of sulfur compounds—namely, aliphatic monothiols and dithiols, with the high oxidation state of myoglobin, known as “ferrylmyoglobin.” The biological significance of ferrylmyoglobin can be viewed in connection with its occurrence in vivo and its potential implications in cardiac and skeletal muscle oxidative conditions. The recovery of myoglobin by thiols, in itself a repair process, generates a thiyl radical species, an important feature of which is its chemical reactivity. Thiyl radicals are potent oxidants, which oxidize vitamin E and ascorbate and are also able to abstract an allylic hydrogen from unsaturated fatty acids, thus initiating lipid peroxidation. Thiyl radical formation appears to be a process inherent in enzymatic reactions, such as the oxidative decarboxylation of pyruvate to acetyl-CoA by pyruvate:ferredoxin oxidoreductase.
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