Anti-UQCRH antibody [EPR9039(B)]

Supplementary info

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

Activity summary

UQCRH also known as ubiquinol-cytochrome c reductase hinge protein plays an important role in the electron transport chain. It forms a part of the core structure of cytochrome bc1 complex (Complex III) in mitochondria. UQCRH has a molecular mass of about 9 kDa and is expressed ubiquitously in human tissues. Its primary role is to assist in transferring electrons by connecting cytochrome c1 and cytochrome c which is essential for cellular respiration and energy production.

Biological function summary

The hinge protein acts as a critical component of the mitochondrial respiratory chain complex III. UQCRH ensures the efficient transfer of electrons within the complex which contributes to generating a proton gradient across the inner mitochondrial membrane. This proton gradient drives ATP synthesis. It is a vital component of the larger respiratory chain complex which is important for aerobic cellular energy metabolism and plays an important role in overall mitochondrial function.

Pathways

UQCRH is a significant player in the oxidative phosphorylation pathway which is central to the production of ATP. The protein closely interacts with components of Complex III and adjacent complexes of the electron transport chain such as NADH dehydrogenase (Complex I) and cytochrome c oxidase (Complex IV). These interactions help UQCRH integrate smoothly within the pathway ensuring the consistent flow of electrons and maintenance of ATP production.

Associated diseases and disorders

UQCRH mutations or dysfunctions link to mitochondrial disorders such as mitochondrial complex III deficiency. Dysfunction in this protein disrupts normal mitochondrial respiration leading to various symptoms including myopathy and encephalopathy. Additionally impaired UQCRH function can contribute to the development of neurodegenerative diseases. Studies have observed connections between abnormal UQCRH activity and proteins such as superoxide dismutase-1 (SOD1) in disease states indicating its possible role in oxidative stress-related pathologies.