ArticleRedox biology2018
Regulation of the mechanism of Type-II NADH: Quinone oxidoreductase from S. aureus.
Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Aminotetrazole-Gold Nanocomplexes Shunt Electrons to Eradicate Bacteria Without ROS-Induced Resistance.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Photoaffinity probe-enabled discovery of sennoside A reductase inJournal of pharmaceutical analysis · 2025Article
- New Insights into the Modification of the Non-Core Metabolic Pathway of Steroids inInternational journal of molecular sciences · 2023Review
- Quinone binding site in a type VI sulfide:quinone oxidoreductase.Applied microbiology and biotechnology · 2022Article
- Inhibition of planktonic growth and biofilm formation ofFrontiers in microbiology · 2022Article
- Catalytic effect of riboflavin on electron transfer from NADH to aquacobalamin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- The catalytic mechanism of electron-bifurcating electron transfer flavoproteins (ETFs) involves an intermediary complex with NAD<sup/>.The Journal of biological chemistry · 2019Article
- The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type-II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains and the only enzymes with NADH:quinone oxidoreductase activity expressed in Staphylococcus aureus (S. aureus), one of the most common causes of clinical infections. NDH-2s are members of the two-Dinucleotide Binding Domains Flavoprotein (tDBDF) superfamily, having a flavin adenine dinucleotide, FAD, as prosthetic group and NAD(P)H as substrate. The establishment of a Charge-Transfer Complex (CTC) between the isoalloxazine ring of the reduced flavin and the nicotinamide ring of NAD+ in NDH-2 was described, and in this work we explored its role in the kinetic mechanism using different electron donors and electron acceptors. We observed that CTC slows down the rate of the second half reaction (quinone reduction) and determines the effect of HQNO, an inhibitor. Also, protonation equilibrium simulations clearly indicate that the protonation probability of an important residue for proton transfer to the active site (D302) is influenced by the presence of the CTC. We propose that CTC is critical for the overall mechanism of NDH-2 and possibly relevant to keep a low quinol/quinone ratio and avoid excessive ROS production in vivo.
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