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The SOD2 enzyme is an important constituent in apoptotic signaling and oxidative stress, most notably as part of the mitochondrial death pathway and cardiac myocyte apoptosis signaling. [11] Programmed cell death is a distinct genetic and biochemical pathway essential to metazoans.
Irwin Fridovich and Joe McCord at Duke University discovered the enzymatic activity of superoxide dismutase in 1968. [5] SODs were previously known as a group of metalloproteins with unknown function; for example, CuZnSOD was known as erythrocuprein (or hemocuprein, or cytocuprein) or as the veterinary anti-inflammatory drug "Orgotein". [6]
Mitochondrial ROS can promote cellular senescence and aging phenotypes in the skin of mice. [11] Ordinarily mitochondrial SOD2 protects against mitochondrial ROS. Epidermal cells in mutant mice with a genetic SOD2 deficiency undergo cellular senescence, nuclear DNA damage, and irreversible arrest of proliferation in a portion of their keratinocytes.
In enzymology, a sulochrin oxidase [(−)-bisdechlorogeodin-forming] (EC 1.21.3.5) is an enzyme that catalyzes the chemical reaction. 2 sulochrin + O 2 2 (−)-bisdechlorogeodin + 2 H 2 O
SOD1 binds copper and zinc ions and is one of three superoxide dismutases responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic and mitochondrial intermembrane space protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide.
SOD1 is located primarily in the cytoplasm, SOD2 in the mitochondria and SOD3 is extracellular. The first is a dimer (consists of two units), while the others are tetramers (four subunits). SOD1 and SOD3 contain copper and zinc ions, while SOD2 has a manganese ion in its reactive centre.
A typical method for establishing PCET pathway is to show that the individual ET and PT pathways operate at higher activation energy than the concerted pathway. [2] The PCETs of SOD2 use PTs between Q143 and a Mn-bound solvent molecule. Deprotonation of Q143 is stabilized with SSHBs shown as yellow-hashed lines.
Superoxide dismutase (SOD) mimetics are synthetic compounds that mimic the native superoxide dismutase enzyme. [1] SOD mimetics effectively convert the superoxide anion (O − 2), a reactive oxygen species, into hydrogen peroxide, which is further converted into water by catalase. [2]