Recombinant Erwinia tasmaniensis NADH-quinone oxidoreductase subunit A (nuoA)

General Properties of NADH-Quinone Oxidoreductase Subunit A

NADH-quinone oxidoreductase subunit A, encoded by the gene nuoA, is part of the NDH-1 complex in bacteria. This complex is simpler than its mammalian counterpart, complex I, but performs a similar function: it shuttles electrons from NADH to quinones via flavin mononucleotide (FMN) and iron-sulfur (Fe-S) centers . The enzyme is located in the inner membrane of bacterial cells and is a multi-pass membrane protein .

Function and Mechanism

The primary function of NADH-quinone oxidoreductase is to couple the electron transfer from NADH to quinones with the translocation of protons across the membrane. This process conserves energy in the form of a proton gradient, which is used by ATP synthase to produce ATP . The subunit A (nuoA) is integral to this process, although its specific role within the complex is less well-defined compared to other subunits like PSST in mitochondrial complex I .

Research Findings and Studies

While specific studies on the recombinant Erwinia tasmaniensis NADH-quinone oxidoreductase subunit A are not readily available, research on similar bacterial systems provides valuable insights. For instance, the bacterial NDH-1 complex, similar to complex I in mitochondria, is sensitive to inhibitors like rotenone and piericidin A, which target specific subunits involved in electron transfer . The PSST subunit in mitochondrial complex I and its bacterial counterpart NQO6 have been identified as key components in electron transfer to quinone .

Comparison with Other Organisms

In bacteria like Escherichia coli, the NDH-1 complex is composed of multiple subunits, including NuoA, and is essential for anaerobic respiration using alternative electron acceptors . The subunit composition and function of NDH-1 in different bacteria can vary, but the core mechanism of electron transfer and proton pumping remains conserved.

Data Tables

Given the lack of specific data on the recombinant Erwinia tasmaniensis NADH-quinone oxidoreductase subunit A, we can provide a general overview of the subunit composition of NDH-1 in a well-studied organism like Escherichia coli:

References ECMDB. NADH-quinone oxidoreductase subunit A (P0AFC3). PNAS. NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron–sulfur cluster N2 to quinone. PMC. Four New Iridoid Metabolites Have Been Isolated from the Stems of Neonauclea reticulata (Havil.) Merr. with Anti-Inflammatory Activities on LPS-Induced RAW264.7 Cells. MetaCyc. NADH:quinone oxidoreductase I, peripheral arm. Nature. Cryo-EM structures of Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae. PMC. Assessment of the Potential Biological Activity of Low Molecular Weight Metabolites of Freshwater Macrophytes with QSAR. BioCyc. Escherichia coli K-12 substr. MG1655 NADH:quinone oxidoreductase subunit F.