Part:BBa_K5210008

SOD

Superoxide dismutase (SOD) acts as an antioxidant enzyme that scavenges oxygen radicals through oxidation/reduction cycles at a very high reaction rate through transition metal ions present at the active site. SOD decomposes O2•− into H2O2 with the release of molecular oxygen. SOD is a kind of enzyme containing Cu, Mn, Zn, and other metal ions. It is widely distributed in plants, animals, and microorganisms [1]. In the process of eliminating free radicals, SOD requires cofactors such as iron, manganese, or copper and zinc to exert maximum catalytic activity when metabolizing toxic intermediates. The metal-binding site is located between the two domains of SOD, and the side chains include aspartate, histamine, and histidine [2]. These cofactors tend to donate electrons to O2•− and regenerate throughout the catalytic mechanism.

Usage and Biology

We learned that ROS are converted to H2O2 by Superoxide dismutase (SOD), and then catalase catalyses the decomposition to H2 O and O2 . We then established a sucrose-sensing switch in Vibrio natriegens, pSacB , which can be activated in the presence of sucrose to express the downstream SOD, catalase to catabolise ROS.

Reference

[1]Zelko, I.N.; Mariani, T.J.; Folz, R.J. Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 2002, 33, 337–349.

[2]Paksi, Z.; Jancsó, A.; Pacello, F.; Nagy, N.; Battistoni, A.; Gajda, T. Copper and zinc binding properties of the N-terminal histidine-rich sequence of Haemophilus ducreyi Cu, Zn superoxide dismutase. J. Inorg. Biochem. 2008, 102, 1700–1710.

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]