NDUFB4 is an accessory subunit of Complex I, which is the first enzyme complex in the mitochondrial electron transport chain. Complex I is responsible for transferring electrons from NADH to ubiquinone, a process that is essential for ATP synthesis through oxidative phosphorylation . Although NDUFB4 is not directly involved in the catalytic activity of Complex I, it is believed to play a role in the structural stability and functional assembly of the complex .
The NDUFB4 gene is located on chromosome 3 and encodes a protein that is approximately 15 kDa in size . The gene has several aliases, including NADH:Ubiquinone Oxidoreductase Subunit B4, Complex I-B15, and CI-B15 . The protein is expressed in various tissues and is essential for normal mitochondrial function .
Mutations or dysfunctions in the NDUFB4 gene can lead to mitochondrial diseases and other disorders. For example, it has been associated with Hantavirus Hemorrhagic Fever with Renal Syndrome and other mitochondrial-related diseases . Understanding the role of NDUFB4 in these conditions can provide insights into potential therapeutic targets.
Recombinant human NDUFB4 protein is often used in research to study its function and role in the mitochondrial respiratory chain. It is typically expressed in Escherichia coli and purified to a high degree of purity (>90%) for use in various biochemical assays . The recombinant protein is useful for studying the structural and functional aspects of Complex I, as well as for developing potential therapeutic interventions .