Recombinant Human SDHD protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The SDHD protein also known as succinate dehydrogenase complex subunit D serves a function in cellular respiration. This protein is a part of the succinate dehydrogenase (SDH) complex found in the inner mitochondrial membrane. This complex is known as complex II in the electron transport chain. The subunit D with a mass of about 15 kDa anchors the larger SDH complex to the membrane and is essential for its structural stability. SDHD is widely expressed in tissues with high energy demands such as the heart liver and muscles.

Biological function summary

The SDH complex has an essential role in both the Krebs cycle and the mitochondrial electron transport chain. SDHD as part of this complex assists in the oxidation of succinate to fumarate an important step in the Krebs cycle. The electrons generated from succinate oxidation are transferred through the SDH complex to ubiquinone contributing to ATP production. The complex facilitates the coupling of the Krebs cycle to the electron transport chain highlighting SDHD’s importance in efficient energy metabolism.

Pathways

SDHD integrates into the Krebs cycle and the electron transport chain linking these vital energy-yielding reactions. In the Krebs cycle it assists in converting succinate to fumarate contributing important intermediates and electron donors for oxidative phosphorylation. It interacts with other components of complex II such as SDHA SDHB and SDHC to facilitate its enzymatic functions. Furthermore its role in electron transport involves ubiquinone which carries electrons to complex III continuing the chain of reactions needed for energy production.

SDHD mutations have been linked with paragangliomas and pheochromocytomas both of which are neuroendocrine tumors. These conditions are associated with disrupted cellular energy metabolism caused by impaired function of the SDH complex. In these tumors mutations in SDHD can lead to a pseudohypoxic state promoting cell proliferation. The protein's dysfunction connects pathophysiologically to related SDHB SDHC and SDHA subunits with mutations in these subunits also contributing to the manifestation of such tumors.