Globin Associated Oxidative Stress

Globins have been studied for their “pseudo-peroxidase” activity for over 70 years, being an ideal model of other kinetically more rapid metalloenzymes. Since those early days of globin redox chemistry research, there has been a realization that globins are much more than oxygen-binding proteins and that they exhibit true redox activities in vivo. Some globins, such as the oxygen-carrying hemoglobin (Hb) of the erythrocyte and myoglobin (Mb) of the myocyte, typically have much of their redox activities suppressed within the confines of the cell. However , under specific conditions, the redox activities of these globins can be manifest, leading to cell and tissue damage through oxidative stress mechanisms including the formation and propagation of free radicals such as the reactive oxygen and nitrogen species (ROS/RNS).