SOD is a very special enzyme, starting with its name. What is “dismutase”? An enzyme that catalyzes (accelerates) a reaction where two equal but opposite reactions occur on two separate molecules. Superoxide dismutase “dismutes” peroxide; it takes two molecules of superoxide, strips the extra electron off one, and places it on the other. So, one molecule ends up with one less electron, forming normal oxygen, and the other ends up with an extra electron. The one with the extra electron rapidly picks up two hydrogen ions to form hydrogen peroxide. In this way, O−2 is converted into two less damaging species.
- 2H++ 2O−2 → O2 + H2O2
Why is Superoxide so dangerous?
Your body is well acquainted with superoxide. Superoxide radicals are part of life, which has been this way since oxygen appeared in the atmosphere thanks to photosynthesis.
We, humans, and most living organisms on Earth depend on oxygen to live. We use oxygen to oxidize food, extracting the energy to keep us going and thinking and writing from that food. This fundamental job of extracting energy from food by oxidizing it to carbon dioxide and water is done in good part by our mitochondria.
Why do we need superoxide dismutases? Why does life need SOD? Because we live in an atmosphere that contains 21% oxygen. Not only that, but most living beings use oxygen, which brings us to what SODs do: they break down superoxides.
How do superoxides form?
Superoxide is a byproduct of mitochondrial respiration and several other enzymes, like xanthine oxidase, that can catalyze the transfer of electrons directly to molecular oxygen under strongly reducing conditions.
What does superoxide do?
It can be a useful weapon against intruders: it is generated by the immune system to kill invading microorganisms. But otherwise, beware of superoxide! A most aggressive oxidant, it can damage molecules like DNA and proteins and structures like cell membranes.
What’s so special about Skin Actives’ protein scavengers of ROS*?
Most skincare products include antioxidants, usually vitamin E or ascorbic acid, or others chosen among the many available botanical antioxidants. At Skin Actives, we use the best antioxidants you see in other brands. The difference is that we also offer purified, high specific* activity, high purity proteins that will help recycle the skin’s natural antioxidant system. Skin Actives’ special antioxidant proteins include superoxide dismutase, catalase, thioredoxin, glutaredoxin, and methionine sulfoxide reductase A and B.
Why antioxidant proteins? Isn’t astaxanthin good enough? Astaxanthin, like carotenes and vitamin C, is good but insufficient to maintain the sophisticated antioxidant cellular system vital for skin health.
What’s special about our new SOD?
It’s the sh-superoxide dismutase-1, a faithful imitation of the human copper/zinc SOD-1 in our body and VERY active. The s stands for synthetic; the h stands for human.
As all our other proteins, shSOD has high specific activity and high purity. sH polypeptide-60 is the INCI for our new SOD, a faithful copy of the enzyme we have in our cells, defending us from aggressive superoxide radicals. The original enzyme resides in the cytosol of our cells and has magnesium and copper.
Why synthetic? Because, by law, the industry can’t use proteins purified from human sources. This protects us from viruses and infections, even from illnesses carried by human sources.
Below is a ribbon representation of the enzyme. Our SOD works as a homodimer, with two identical subunits. Specific activity depends on how well the activity has been preserved during production and purification. Still, the catalytic capacity of the enzyme, which depends on its structure and function, is paramount. In the case of the human SOD-1, the activity is very high, >500 kU/mg. Usually, I would compliment Skin Actives scientists for their ability to obtain the highest possible specific activity, but in this case it’s also the beautiful architecture of this enzyme that makes it so efficient.
Figure. A ribbon representation of superoxide dismutase-1. By Emw – CC BY-SA 3.0, https://commons.wikimedia.org/w/index.php?curid=8821646. Structure and mechanism are described in Tainer et al. 1983.
*High specific activity proteins: Proteins can lose activity. It is possible to have a protein that is totally inactivated (like when you boil an egg), and an inactivated enzyme is worthless.
*High purity. You can add a ton of protein but if only a small fraction of that protein is the enzyme you want, you are wasting your time. This is what happens when you use “melon SOD”, which is melon juice with almost undetectable SOD activity.
Add antioxidants to your DIY formulation
Search the keyword antioxidant on our website for actives that will enrich your DIY product, making it better than anything you can find in a department store—starting with ascorbic acid and derivatives (our favorite: magnesium ascorbyl phosphate), antioxidant booster, R-alpha lipoic acid, ferulic acid, vitamin E oil, kakadu plum, amla extract (in Indian food stores), and so much more. Don’t forget the ROS* BioNet!
An update: our sH-superoxide dismutase-1 now has an INCI name: sH-polypeptide-60
Note for professional formulators: For specific applications, we offer an enzyme that, with the switch of a single amino acid, acquires resistance to high temperature.
Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. doi: 10.1038/306284a0. PMID: 6316150.
Kurahashi, T., & Fujii, J. (2015). Roles of Antioxidative Enzymes in Wound Healing. Journal of Developmental Biology, 3(2), 57–70. doi:10.3390/jdb3020057
Iuchi, Y.; Roy, D.; Okada, F.; Kibe, N.; Tsunoda, S.; Suzuki, S.; Takahashi, M.; Yokoyama, H.; Yoshitake, J.; Kondo, S.; et al. Spontaneous skin damage and delayed wound healing in SOD1-deficient mice. Mol. Cell. Biochem. 2010, 341, 181–194
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