Recombinant Human NDUFA1 protein

Supplementary info

Activity summary

NDUFA1 also called NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 is a critical component of the mitochondrial respiratory chain. It has an approximate molecular mass of 5.5 kDa and resides within the inner mitochondrial membrane. This protein is part of the larger NADH:ubiquinone oxidoreductase also known as Complex I which is present across various tissues where energy production is essential. NDUFA1 aids the proper function of Complex I to facilitate electron transfer during cellular respiration.

Biological function summary

NDUFA1 plays an integral role in the electron transfer process by linking with other subunits to form the Complex I assembly. It is important for the initial step of the electron transport chain where it helps in transferring electrons from NADH to ubiquitin. This step is important as it contributes to the generation of a proton gradient across the mitochondrial membrane which is necessary for ATP synthesis. Part of the mitochondrial enzymatic pathway NDUFA1 works in concert with other enzyme complexes to maintain cellular energy balance.

Pathways

NDUFA1 engages primarily in the oxidative phosphorylation pathway which is pivotal for ATP production in cells. This pathway connects NDUFA1 with other complexes such as Complex II Complex III and Complex IV ensuring comprehensive electron flow and proton gradient creation. In addition NDUFA1 is involved in the mitochondrial electron transport chain linking with proteins such as cytochrome c for maintaining energy metabolism and cellular respiration.

Associated diseases and disorders

Mutations or dysfunctions in NDUFA1 relate to mitochondrial disorders like Leigh syndrome which affect energy-dependent tissues such as the brain and muscles. Such mutations lead to impaired electron transfer therefore causing energy deficits. NDUFA1 mutations can also contribute to cardiac and neurological disorders due to disrupted ATP synthesis. Within these diseases NDUFA1 interacts with other defective proteins of the mitochondrial respiratory chain exacerbating metabolic irregularities and contributing to disease pathogenesis.