NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). Plays a critical role in M.tuberculosis ability to inhibit apoptosis of infected macrophages; thus helps the bacterium in its struggle to resist the host immune response (PubMed:17658950). In fact, via a NuoG-dependent mechanism, M.tuberculosis can neutralize NOX2-derived reactive oxygen species (ROS) in order to inhibit TNF-alpha-mediated host cell apoptosis (PubMed:20421951). Also mediates inhibition of neutrophil apoptosis, leading to delayed activation of naive CD4 T cells (PubMed:22264515). a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) Binds 1 [2Fe-2S] cluster per subunit. Binds 3 [4Fe-4S] clusters per subunit. The type I NADH dehydrogenase consists of 14 different subunits. Deletion of nuoG in M.tuberculosis reduces its ability to inhibit apoptosis of infected human or mouse macrophages and significantly decreases its virulence in mice (PubMed:17658950). The apoptogenic phenotype of the mutant strain is significantly reduced in human macrophages treated with caspase-3 and -8 inhibitors, TNF-alpha-neutralizing antibodies, and also after infection of murine TNF(-/-) macrophages. Moreover, incubation of macrophages with inhibitors of reactive oxygen species (ROS) reduces not only the apoptosis induced by the nuoG deletion mutant, but also its capacity to increase macrophage TNF-alpha secretion. The phagosomes infected with the mutant show increased ROS levels compared to M.tuberculosis phagosomes in primary murine and human alveolar macrophages. The increase in nuoG deletion mutant induced ROS and apoptosis is abolished in NOX-2 deficient (gp91(-/-)) macrophages (PubMed:20421951). Compared to wild-type, the nuoG deletion mutant spreads to a larger number of lung phagocytic cells. Consistent with the shorter lifespan of infected neutrophils, infection with the nuoG mutant results in fewer bacteria per infected neutrophil, accelerated bacterial acquisition by dendritic cells, earlier trafficking of these dendritic cells to lymph nodes, and faster CD4 T cell priming. Neutrophil depletion abrogates accelerated CD4 T cell priming by the nuoG mutant, suggesting that inhibiting neutrophil apoptosis delays adaptive immunity in tuberculosis (PubMed:22264515). Belongs to the complex I 75 kDa subunit family.