Globins may scavenge, generate, or sense ROS and RNS as part of their physiological role. The redox activity of members of the wider family of globins, such as neuroglobin, cytoglobin, and many more, also have important associations with the mechanisms of cell stress and stress response and can be key regulators of signaling molecules for a variety of processes. This includes the formation of radicals and radical-like species, including reactive oxygen and nitrogen species (ROS/RNS). However, under certain conditions, the redox activities of these globins can thrive, leading to cell and tissue damage through oxidative stress mechanisms. The redox activities of some globins, such as oxygen-carrying hemoglobin and myoglobin, are typically suppressed within the confines of the cell. Since those early days of globin redox chemistry research, there has been a realization that globins exhibit true in vivo redox activities. Globins have been studied for their “pseudo-peroxidase” activity for over 70 years, being an ideal model of other kinetically more-rapid metalloenzymes.
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