ArticleBiochimica et biophysica acta2014
Characterization of the type 2 NADH:menaquinone oxidoreductases from Staphylococcus aureus and the bactericidal action of phenothiazines.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 63 citations in OpenAlex.
- Cryptotanshinone inhibitsVirulence · 2026Article
- α-Mangostin Competing the Menaquinone-Binding Sites of NDH-2 to Block the Electron Transfer at the Quinone Pool ofAntibiotics (Basel, Switzerland) · 2026Article
- Mechanisms of action of the hexane extract ofADMET & DMPK · 2026Article
- Article
- Antibacterial and antibiofilm efficacy of TMC647055 against methicillin-resistant Staphylococcus aureus.Archives of microbiology · 2025Article
- STOP Strategy to InhibitAntibiotics (Basel, Switzerland) · 2025Article
- Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.Current protein & peptide science · 2025Review
- Synthetic indole derivatives as an antibacterial agent inhibiting respiratory metabolism of multidrug-resistant gram-positive bacteria.Communications biology · 2024Article
- Myricetin Acts as an Inhibitor of Type II NADH Dehydrogenase fromMolecules (Basel, Switzerland) · 2024Article
- The respiratory chain ofFrontiers in microbiology · 2024Article
- Quinone Pool, a Key Target of Plant Flavonoids Inhibiting Gram-Positive Bacteria.Molecules (Basel, Switzerland) · 2023Article
- Article
- Uracil restores susceptibility of methicillin-resistantFrontiers in pharmacology · 2023Article
- Development of Phenothiazine Hybrids with Potential Medicinal Interest: A Review.Molecules (Basel, Switzerland) · 2022Review
- Review
- Article
- New Insights Into the Antibacterial Mechanism of Cryptotanshinone, a Representative Diterpenoid Quinone FromFrontiers in microbiology · 2021Article
- Role of respiratory NADH oxidation in the regulation of Staphylococcus aureus virulence.EMBO reports · 2020Article
- Revealing the Membrane-Bound Catalytic Oxidation of NADH by the Drug Target Type-II NADH Dehydrogenase.Biochemistry · 2019Article
- Respiration and Small Colony Variants ofMicrobiology spectrum · 2019Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Methicillin-resistant Staphylococcus aureus (MRSA) is currently one of the principal multiple drug resistant bacterial pathogens causing serious infections, many of which are life-threatening. Consequently, new therapeutic targets are required to combat such infections. In the current work, we explore the type 2 Nicotinamide adenine dinucleotide reduced form (NADH) dehydrogenases (NDH-2s) as possible drug targets and look at the effects of phenothiazines, known to inhibit NDH-2 from Mycobacterium tuberculosis. NDH-2s are monotopic membrane proteins that catalyze the transfer of electrons from NADH via flavin adenine dinucleotide (FAD) to the quinone pool. They are required for maintaining the NADH/Nicotinamide adenine dinucleotide (NAD(+)) redox balance and contribute indirectly to the generation of proton motive force. NDH-2s are not present in mammals, but are the only form of respiratory NADH dehydrogenase in several pathogens, including S. aureus. In this work, the two putative ndh genes present in the S. aureus genome were identified, cloned and expressed, and the proteins were purified and characterized. Phenothiazines were shown to inhibit both of the S. aureus NDH-2s with half maximal inhibitory concentration (IC50) values as low as 8μM. However, evaluating the effects of phenothiazines on whole cells of S. aureus was complicated by the fact that they are also acting as uncouplers of oxidative phosphorylation. This article is part of a Special Issue entitled: 18th European Bioenergetic Conference.
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