ReviewMicrobiology and molecular biology reviews : MMBR2004
New insights into type II NAD(P)H:quinone oxidoreductases.
Review in Microbiology and molecular biology reviews : MMBR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
114 citing papers in PubMed, 273 citations in OpenAlex.
- Aminotetrazole-Gold Nanocomplexes Shunt Electrons to Eradicate Bacteria Without ROS-Induced Resistance.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- A Bacillales-specific tubular scaffold essential for NADH dehydrogenase activity.Nature communications · 2026Article
- BN-PAGE of Ustilago maydis Respiratory Complexes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- Identification of OxyR as an activator of type 1 fimbriae (Microbiology spectrum · 2025Article
- Carabrone inhibits Gaeumannomyces tritici growth by targeting mitochondrial complex I and destabilizing NAD⁺/NADH homeostasis.PLoS pathogens · 2025Article
- Crp and Arc system directly regulate the transcription of NADH dehydrogenase genes inMicrobiology spectrum · 2025Article
- Article
- Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.Current protein & peptide science · 2025Review
- Alternative oxidase blunts pseudohypoxia and photoreceptor degeneration due to RPE mitochondrial dysfunction.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Scrutinizing aApplied and environmental microbiology · 2024Article
- A novel inhibitor of the mitochondrial respiratory complex I with uncoupling properties exerts potent antitumor activity.Cell death & disease · 2024Article
- Identification of MIMAS, a multifunctional mega-assembly integrating metabolic and respiratory biogenesis factors of mitochondria.Cell reports · 2024Article
- Specific growth rates and growth stoichiometries of Saccharomycotina yeasts on ethanol as sole carbon and energy substrate.FEMS yeast research · 2024Article
- Quantitative proteomics reveals oxygen-induced adaptations inFrontiers in microbiology · 2024Article
- Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases ofFrontiers in microbiology · 2024Article
- The respiratory chain ofFrontiers in microbiology · 2024Article
- Genomic investigations of diverse corbiculate bee gut-associated Gilliamella reveal conserved pathways for energy metabolism, with diverse and variable energy sources.Access microbiology · 2024Article
- Integrated chemical and genetic screens unveil FSP1 mechanisms of ferroptosis regulation.Nature structural & molecular biology · 2023Article
- NRF2, a Superstar of Ferroptosis.Antioxidants (Basel, Switzerland) · 2023Review
54 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type II NAD(P)H:quinone oxidoreductases (NDH-2) catalyze the two-electron transfer from NAD(P)H to quinones, without any energy-transducing site. NDH-2 accomplish the turnover of NAD(P)H, regenerating the NAD(P)(+) pool, and may contribute to the generation of a membrane potential through complexes III and IV. These enzymes are usually constituted by a nontransmembrane polypeptide chain of approximately 50 kDa, containing a flavin moiety. There are a few compounds that can prevent their activity, but so far no general specific inhibitor has been assigned to these enzymes. However, they have the common feature of being resistant to the complex I classical inhibitors rotenone, capsaicin, and piericidin A. NDH-2 have particular relevance in yeasts like Saccharomyces cerevisiae and in several prokaryotes, whose respiratory chains are devoid of complex I, in which NDH-2 keep the balance and are the main entry point of electrons into the respiratory chains. Our knowledge of these proteins has expanded in the past decade, as a result of contributions at the biochemical level and the sequencing of the genomes from several organisms. The latter showed that most organisms contain genes that potentially encode NDH-2. An overview of this development is presented, with special emphasis on microbial enzymes and on the identification of three subfamilies of NDH-2.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.