NDH-1, also known as Complex I, is a multi-subunit enzyme critical for energy metabolism in bacteria. Subunit K (nuoK2) is one of the 14 essential subunits in G. uraniireducens, contributing to the structural and functional integrity of the enzyme. Key roles include:
Electron Transfer: Facilitates the transfer of electrons from NADH to ubiquinone via a series of redox-active cofactors (e.g., FMN, Fe-S clusters) .
Proton Translocation: Couples redox reactions to the translocation of protons across the membrane, generating a proton gradient for ATP synthesis .
Expression System: Typically expressed in Escherichia coli using optimized vectors for heterologous protein production .
Purification: Purified via affinity chromatography (e.g., His-tagged variants) .
Storage:
| Subunit | Function | Cofactors | Proton Translocation |
|---|---|---|---|
| nuoK2 | Structural support for electron transfer | None | Indirect |
| nuoB/C | FMN covalently bound, electron transfer | FMN | Direct |
| nuoI/L/M | Fe-S clusters, proton translocation | Fe-S clusters | Direct |
Note: Data synthesized from general NDH-1 studies .
Structural Data: No high-resolution crystal or cryo-EM structures of G. uraniireducens nuoK2 are reported.
Functional Assays: Kinetic parameters (e.g., k<sub>cat</sub>, K<sub>m</sub>) for NADH oxidation or proton pumping remain uncharacterized.
KEGG: gur:Gura_4234
STRING: 351605.Gura_4234