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From Proteopedia

Succinate dehydrogenase is an important enzyme in the citric acid cycle that converts succinate to fumarate, two intermediate carbon compounds in the cycle. Succinate dehydrogenase is an integrated membrane protein that exists in the inner membrane of the mitochondria. This diagram shows two enzymes in a complex working together from Gallus gallus, the common chicken. The individual enzyme exists as a . The of the enzyme is primarily alpha helices, illustrated in red, and beta sheets, illustrated in blue. There is also non-repetitive coil, seen in white. of the backbone are visible in black. The pattern of hydrogen bonding on the beta sheets indicates that they are anti-parallel. This enzyme contains no sulfide bonds responsible for stabilizing tertiary structure. The for succinate dehydrogenase are illustrated here; grey represents the hydrophobic side chain residues, and orange represents charged and hydrophilic side chain residues. This transmembrane enzyme has contact with the at the end of the protein that exists outside the membrane. In this figure, water molecules are illustrated in dark blue. The , seen in pink, interact at multiple points on the enzyme. The enzyme has at various side chain residues, represented in dark blue. These residues of contact are polar or charged, and this helps to stabilize the oxygenated ligand, succinate, for its catalysis. The primary residue is illustrated in red.