succinate dehydrogenase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor. [RHEA:16357]

Succinate dehydrogenase (SDH), also known as respiratory complex II, is a key enzyme in the mitochondrial electron transport chain. It catalyzes the oxidation of succinate to fumarate, a step in the citric acid cycle, and simultaneously reduces ubiquinone (Q) to ubiquinol (QH2). This process involves the transfer of electrons from succinate to FAD (flavin adenine dinucleotide) within the enzyme, followed by the transfer of electrons to an iron-sulfur cluster and finally to ubiquinone. SDH is a transmembrane protein complex embedded in the inner mitochondrial membrane, composed of four subunits: SDHA, SDHB, SDHC, and SDHD. SDHA and SDHB are involved in the catalytic activity, while SDHC and SDHD anchor the complex to the membrane and facilitate electron transfer. The enzyme plays a crucial role in energy production by coupling the oxidation of succinate to the reduction of ubiquinone, thereby contributing to the generation of a proton gradient across the inner mitochondrial membrane that is essential for ATP synthesis.'
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Proteins (1)

Compounds (1)