Sdh Activity Lab Report
The Impact of Malonate on SDH Activity
Hypothesis:
We hypothesize that the reagent malonate will inhibit, or decrease SDH activity.
Justification:
Succinic dehydrogenase is an enzyme that is bound to the inner membrane of the mitochondria and takes part in the Krebs Cycle as well as the Electron Transport Chain. Most importantly, SDH is a major component in the Krebs Cycle, and catalyzes the oxidation of its succinate ions to fumarate ions, changing its chemical composition from C4H4O4 to C4H2O4, by removing hydrogen ions. ("5. Enzyme Inhibitors,” 2013).
The introduction of malonate can decrease succinic dehydrogenase activity by acting as an inhibitor. This is because the malonate will block the substrate succinate from reaching the enzyme. The result of this interaction yields no product and succinic dehydrogenase activity decreases. This type of inhibition can be called competitive because only one of the substrates can bind to the enzyme. In a study conducted at the McArdle Memorial Laboratory in Wisconsin, researchers found that the malonate did not damage the enzyme because the enzyme-substrate complex was similar to that of succinate. Malonate has the chemical composition C3H2O4-2 compared to the C4H4O4 composition of succinic dehydrogenase (Potter and Dubois, 1943).
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In a study from 2013 diazoxide and malonate were both used to test succinic dehydrogenase activity in the mitochondria of wild mice. Both diazoxide and malonate inhibited succinic dehydrogenase activity in the mitochondria of wild-type mice. Tests showed that malonate and diazoxide both decreased succinic dehydrogenase activity, however malonate decreased succinic dehydrogenase activity at a lower rate than diazoxide. Malonate absorbance showed to decrease approximately ten percent, whereas diazoxide absorbance decreased approximately fifty percent. (Anastacio, et. al.
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