Understand more about the critical role of superoxide

The superoxide dismutase family of enzymes catalyzes the rapid conversion of superoxide to molecular oxygen and hydrogen peroxide, which itself is subsequently converted to molecular oxygen and water.

Normal dismutase activity

Under ideal metabolic conditions, superoxide dismutase enzymes remove superoxide before it can enter undesirable oxygen metabolic pathways and thus protect the organism from the damaging effects of oxidative stress. In this process, dismutases convert superoxide to molecular oxygen and hydrogen peroxide and allow the body to sustain healthy cellular activity.1

Dismutase activity in reaction to excessive oxidative stress

Under conditions of excessive oxidative stress, such as occurs with the administration of radiation, cellular mechanisms for its normal removal (including superoxide dismutase enzymes) may be overwhelmed. This results in superoxide reacting with other molecules, such as nitric oxide or ferric iron, and initiating undesired oxygen metabolic pathways.2

How do dismutase mimetics work?

Our small-molecule dismutase mimetics are designed to replicate superoxide dismutase activity and thus fill the gap in this critical activity when overwhelmed by excess superoxide, whether caused by disease or some insult like radiation.

Performing the same function as the naturally occurring superoxide dismutase enzymes, our drugs are distinguished as being the only small molecules that truly mimic the native enzymatic activity.

References:
1. Perry JJ, Shin DS, Getzoff ED, Tainer JA. The structural biochemistry of the superoxide dismutases. Biochim Biophys Acta. 2010;1804(2):245-262.
2. Conklin KA. Chemotherapy-associated oxidative stress: impact on chemotherapeutic effectiveness. Integr Cancer Ther. 2004;3(4):294-300.