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Key
Succinate dehydrogenase, which catalyzes succinate oxidation to fumarate, is the only enzyme in the tricarboxylic acids cycle that is not free in the mytochondrial matrix: it is an integral membrane protein. Its substrate transfers two electrons to a flavin adenine dinucleotide ( FAD). One by one, those electrons are then transfered by Fe-S clusters to a heme , which donates two electrons to a lipid-soluble molecule, ubiquinone (Q), converting it in ubiquinol (QH2). Since the succinate/fumarate redox potential is very close to that of the Q/QH2 pair, the free energy change in this step is not enough to pump electrons from the matrix to the intermembrane space. Other interactive models: NADH dehidrogenase Cytochrome bc1 complex Cytochrome c oxidase Succinate dehidrogenase Anti-parallel β-sheet α-helix Parallel β-sheet Hemoglobin Oxyhemoglobin (I) Oxyhemoglobin (II) Metabolic pathways: Fermentation and respiration Fatty acids metabolism Glycolysis Citric acid cycle Glycogen synthesis and glycogenolysis Gluconeogenesis Aminoacid degradation and urea cycle Pentose phosphate pathway Metabolic regulation and integration visitas desde 4 de Janeiro de 2002
Other interactive models: NADH dehidrogenase Cytochrome bc1 complex Cytochrome c oxidase Succinate dehidrogenase Anti-parallel β-sheet α-helix Parallel β-sheet Hemoglobin Oxyhemoglobin (I) Oxyhemoglobin (II) Metabolic pathways: Fermentation and respiration Fatty acids metabolism Glycolysis Citric acid cycle Glycogen synthesis and glycogenolysis Gluconeogenesis Aminoacid degradation and urea cycle Pentose phosphate pathway Metabolic regulation and integration
NADH dehidrogenase Cytochrome bc1 complex Cytochrome c oxidase Succinate dehidrogenase Anti-parallel β-sheet α-helix Parallel β-sheet Hemoglobin Oxyhemoglobin (I) Oxyhemoglobin (II)
Fermentation and respiration Fatty acids metabolism Glycolysis Citric acid cycle Glycogen synthesis and glycogenolysis Gluconeogenesis Aminoacid degradation and urea cycle Pentose phosphate pathway Metabolic regulation and integration
visitas desde 4 de Janeiro de 2002