iron

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DFO action was suggested due to its ability to inhibit the oxidative stress induced by excess iron and reduce ferryl myoglobin which is oxidized myoglobin aggregates that produce oxidative damage [46].
The studies have been continued by Szklarz and collaborators [28,33], who found a correlation between the numbers of docked orientations within 4 A of the ferryl oxygen and experimentally determined metabolite ratios.
This method is based on the interaction of the phenothiazine compound 2,27-azino-di[3-ethylbenthiazoline sulphonate] (ABTS) with ferryl myoglobin, produced through the reaction of the [ABTS.sup.*+] radical, which can be monitored by reading absorbance at 750 nm or 405 nm.
For example, the recent clinical trial showed that blocking ferryl hemoglobin with acetaminophen improved sepsis outcome [75].
The principle of the antioxidant assay is based on the formation of a ferryl myoglobin radical from metmyoglobin and hydrogen peroxide, which oxidizes the 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) to produce a radical cation, [ABTS.sup.+], a soluble chromogen that is green in color and can be measured in a spectrophotometer at 405 nm.
Mb and Hb can peroxidate lipids in the ferryl oxidation state by removing hydrogen from the polyunsaturated fatty acids.