sdh lab (1)

sdh lab (1) - The Inhibitory Action Of Oxaloacetate on SDH...

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Raelyn Loftis, Nikita Nagaraj, Eleni Papanikolaou and Harpreet Singh Introduction Succinate Dehydrogenase (SDH) is a mitochondrial enzyme found in the inner membrane of the organelle. It plays a vital role in cellular respiration, specifically in the Kreb’s cycle and the Electron transport cycle (ETC). In the Kreb’s cycle the oxidation of succinate to fumerate is catalyzed by SDH and the reduction of ubiquinone to ubiquinol is also done by the same. ( Szetzo,Weng, Seung, summary) This enzyme has a bound coenzyme, Flavine Adenine Dinucleotide (FAD) which accepts electrons donated by the oxidation of succinate, thus, getting reduced from FAD to FADH2. Since all enzymes need to be recycled for further activity FADH2 has to lose its extra electrons to be regenerated to FAD. FAD is tightly bound to SDH and it can only pass down the electrons to the ETC. These electrons are passed down the chain and ultimately given to the terminal electron acceptor, oxygen. The activity of a certain enzyme can be determined by measuring its protein concentration. In particular, to measure the activity of SDH, the ETC needs to be short circuited. The ETC block leads to a build up of FADH2. An artificial electron acceptor, 2,6-dichlorophenolindophenol (DCPIP) can be used to accept the electrons and assess the relative SDH enzyme activity. DCPIP is a dye, that has a different in absorbance when in oxidized and reduced state. (Stanford, p. 3) The Bradford Assay method is used to determine the protein concentration in this experiment. Oxaloacetate……. General info on just oxaloacetate
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sdh lab (1) - The Inhibitory Action Of Oxaloacetate on SDH...

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