Recombinant Ochrobactrum anthropi NADH-quinone oxidoreductase subunit K (nuoK)
Description
Electron Transport Activity
nuoK participates in the NADH dehydrogenase complex, which transfers electrons from NADH to quinones (e.g., ubiquinone) in the bacterial inner membrane. This process is coupled to proton translocation, contributing to ATP synthesis .
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Catalytic Mechanism: Facilitates electron transfer via coordination with other subunits (e.g., nuoB, nuoH) and flavin cofactors .
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Substrate Specificity: Primarily reduces quinones but may interact with other electron acceptors under stress conditions .
Comparative Analysis with Related Proteins
| Protein | Organism | Key Differences |
|---|---|---|
| Helicobacter pylori nuoK | Helicobacter pylori | Amino acid sequence differs (e.g., Q1CRZ1 vs. O. anthropi A6X1M3) |
| NQO1 (DT-diaphorase) | Humans | Uses NAD(P)H and NRH as cofactors; lacks proton translocation |
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ELISA Kits: Used to detect nuoK-specific antibodies in serological studies .
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Enzyme Kinetics: Studied in vitro to elucidate electron transfer mechanisms and inhibitor binding (e.g., dicoumarol) .
Ochrobactrum anthropi as a Host Organism
O. anthropi is a Gram-negative, urease-positive bacterium associated with opportunistic infections in immunocompromised patients . Its genome includes plasmids encoding transporters and metabolic genes, which may enhance survival in diverse environments .
Relevance of nuoK in O. anthropi
While nuoK is not directly linked to virulence, its role in energy metabolism underscores the importance of Complex I in bacterial adaptation. Mutations in analogous subunits (e.g., NQO1 in humans) are associated with reduced enzyme stability and disease susceptibility .
Challenges and Future Directions
Product Specs
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Target Background
NDH-1 (NADH-quinone oxidoreductase subunit K) facilitates electron transfer from NADH to quinones within the respiratory chain, utilizing FMN and iron-sulfur (Fe-S) centers as intermediaries. In this organism, ubiquinone is believed to be the primary electron acceptor. This redox reaction is coupled with proton translocation; for every two electrons transferred, four protons are translocated across the cytoplasmic membrane, thus establishing a proton gradient that conserves redox energy.
KEGG: oan:Oant_2413
STRING: 439375.Oant_2413
