Recombinant Human NDUFB8 protein (GST tag N-Terminus)

Supplementary information

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

The NDUFB8 protein also known as NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 is an integral component of the mitochondrial inner membrane. It is a part of the electron transport chain and plays a role in mitochondrial oxidative phosphorylation. NDUFB8 has a molecular weight of approximately 19 kDa. It is broadly expressed in tissues with high-energy demands like the heart brain skeletal muscle and liver. This expression indicates its significant involvement in energy metabolism.

Biological function summary

NDUFB8 is an accessory subunit of the mitochondrial Complex I the largest enzyme of the respiratory chain. It assists in the transfer of electrons from NADH to ubiquinone a critical step in cellular respiration that contributes to ATP production. Though not directly involved in catalysis its presence is essential for the structural integrity and assembly of Complex I. By maintaining this complex's structure NDUFB8 helps ensure efficient energy production in cells.

Pathways

NDUFB8 participates in the oxidative phosphorylation pathway playing a significant role in the mitochondrial respiratory chain. It influences the production of ATP the primary energy carrier in cells. Its association with Complex I links it to other subunits and proteins like NDUFA9 and NDUFA1 in the same pathway. These connections emphasize NDUFB8's importance within the pathway and its contribution to cellular energy management.

Dysfunction in NDUFB8 is linked to mitochondrial disorders often resulting in neurological diseases or muscle weakness such as Leigh syndrome. Mutations affecting NDUFB8 or its associated proteins like NDUFA13 could disrupt the assembly or function of Complex I leading to impaired energy production. This connection highlights the role of NDUFB8 in maintaining cellular energy balance and its impact on health when malfunctioning.