ArticleJournal of bacteriology2001
H(2)O(2)-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Mechanistic insights into redox activity and catalytic determinants of the haloarchaeal flavin-dependent oxidoreductasebioRxiv : the preprint server for biology · 2026Article
- Characteristics of a water-forming NADH oxidase from Methanobrevibacter smithii, an archaeon in the human gut.Bioscience reports · 2016Article
- Involvement of NADH Oxidase in Competition and Endocarditis Virulence in Streptococcus sanguinis.Infection and immunity · 2016Article
- Carboxydotrophic growth of Geobacter sulfurreducens.Applied microbiology and biotechnology · 2016Article
- A Hidden Transhydrogen Activity of a FMN-Bound Diaphorase under Anaerobic Conditions.PloS one · 2016Article
- NADH: flavin oxidoreductase/NADH oxidase and ROS regulate microsclerotium development in Nomuraea rileyi.World journal of microbiology & biotechnology · 2014Article
- Characterization of NADH oxidase/NADPH polysulfide oxidoreductase and its unexpected participation in oxygen sensitivity in an anaerobic hyperthermophilic archaeon.Journal of bacteriology · 2010Article
- Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum.FEBS letters · 2009Article
- Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus.Archaea (Vancouver, B.C.) · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An enzyme exhibiting NADH oxidase (diaphorase) activity was isolated from the hyperthermophilic sulfate-reducing anaerobe Archaeoglobus fulgidus. N-terminal sequence of the protein indicates that it is coded for by open reading frame AF0395 in the A. fulgidus genome. The gene AF0395 was cloned and its product was purified from Escherichia coli. Like the native NADH oxidase (NoxA2), the recombinant NoxA2 (rNoxA2) has an apparent molecular mass of 47 kDa, requires flavin adenine dinucleotide for activity, has NADH-specific activity, and is thermostable. Hydrogen peroxide is the product of bivalent oxygen reduction by rNoxA2 with NADH. The rNoxA2 is an oxidase with diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c. During purification NoxA2 remains associated with the enzyme responsible for D-lactate oxidation, the D-lactate dehydrogenase (Dld), and the genes encoding NoxA2 and Dld are in the same transcription unit. Together these results suggest that NADH oxidase may be involved in electron transfer reactions resulting in sulfate respiration.
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