Recombinant Pisaster ochraceus NADH-ubiquinone oxidoreductase chain 4L (ND4L)
Description
Functional Role in Mitochondrial Complex I
ND4L is essential for Complex I assembly and activity. Studies in Chlamydomonas reinhardtii demonstrate that the absence of ND4L disrupts the 950-kDa Complex I structure and abolishes enzyme activity . In humans, the homologous MT-ND4L gene encodes a mitochondrial-encoded subunit critical for electron transport chain efficiency .
Key Functional Insights:
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Electron Transport: ND4L stabilizes interactions between hydrophilic and hydrophobic domains of Complex I, enabling NADH-to-ubiquinone electron transfer .
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Assembly Dependency: Hydrophobic subunits like ND4L are necessary for proper Complex I folding and membrane integration .
Comparative Insights from Model Organisms
While ND4L in Pisaster ochraceus is recombinant, its function mirrors endogenous subunits in other species:
Critical Considerations for Handling and Use
Product Specs
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Target Background
A core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). It's considered part of the minimal assembly required for catalytic activity. Complex I facilitates electron transfer from NADH to the respiratory chain, with ubiquinone believed to be the immediate electron acceptor.
