Enzymes are described as the organic catalysts, which increase the rate of reaction of a biochemical reaction. Enzymes are proteins that speed up the rate of reaction without being used up, and therefore they are reusable (Jonathan, 2012). The enzyme studied in this lab was succinate dehydrogenase.
Enzyme kinetics is the study of how biological catalysts increase the reaction rate in reactions. Without the catalysts, the biological procedures necessary for organisms would not continue at a rate that could sustain life. A more simpler way to model enzyme kinetics is the Michealis-Menten model (Wilkinson, 1970). This model describes the rate of enzyme reactions, by relating the reaction rate to concentration of the substrate. Reaction rates can be represented mathematically, which demonstrates how the different chemical species involved in the reaction are affected throughout the reaction (Wilkinson, 1970).
The Mitochondria and Electron Transport Chain
The mitochondria is found in the cytoplasm of almost all eukaryotic cells, and its primary function is to generate a large amount of energy in the form of ATP (adenosine triphosphate) (Morris et al., 2013). ATP is then used to carry out other cellular processes. The mitochondrial matrix contains DNA on the genome and the enzymes of the krebs cycle, which metabolizes nutrients into by-products that the mitochondria can use for energy making (Metabolism, 2014).
In the mitochondria, the conversion of succinate to fumerate (by the use of succinate dehydrogenase and FAD) is required to generate the proton gradient. Succinate is a chemical that is produced in the ATC cycle for cellular respiration, while succinate dehydrogenase (SDH) is one of the only enzymes that is used ...
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... It states that the initial velocity should be directly proportional to the volume of mitochondrial suspension (Fig. 2 & 4). There is a higher initial velocity of the reaction because of the SDH’s “want” to attract to the succinate. With the increasing amount of SDH concentrations in tubes 1 to 4 in figure 2, the binding of succinate to SDH will increase (Jonathan et al., 2012). Tube 1 has the least amount of SDH concentration and therefore shows the lowest initial velocity, whereas tube 4 had the highest SDH concentration and showed a higher initial velocity (Fig. 2).
According to the results and the data we have collected, we are able to conclude that as SDH concentration increases, the reaction rate from succinate to fumarate also increases. Figures 2 and 3 prove that with the addition of malonate and the omitted succinate and azide, slow down the reaction rate.
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