ArticleBiochimica et biophysica acta2008
Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4.
Article in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- How methanotrophs respond to pH: A review of ecophysiology.Frontiers in microbiology · 2022Review
- Open Issues for Protein Function Assignment inGenes · 2021Article
- The aerobic respiratory chain of Pseudomonas aeruginosa cultured in artificial urine media: Role of NQR and terminal oxidases.PloS one · 2020Article
- Mutational loss of carotenoids in alkaliphilicMicrobiology (Reading, England) · 2019Article
- Article
- Contribution of intracellular negative ion capacity to Donnan effect across the membrane in alkaliphilic Bacillus spp.Journal of bioenergetics and biomembranes · 2016Article
- Characterization of the type 2 NADH:menaquinone oxidoreductases from Staphylococcus aureus and the bactericidal action of phenothiazines.Biochimica et biophysica acta · 2014Article
- Cardiolipin is dispensable for oxidative phosphorylation and non-fermentative growth of alkaliphilic Bacillus pseudofirmus OF4.The Journal of biological chemistry · 2014Article
- The respiratory chains of four strains of the alkaliphilic Bacillus clausii.FEBS open bio · 2014Article
- The composition of the Bacillus subtilis aerobic respiratory chain supercomplexes.Journal of bioenergetics and biomembranes · 2012Article
- Relationship between rates of respiratory proton extrusion and ATP synthesis in obligately alkaliphilic Bacillus clarkii DSM 8720(T).Journal of bioenergetics and biomembranes · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A putative Type II NADH dehydrogenase from Halobacillus dabanensis was recently reported to have Na+/H+ antiport activity (and called Nap), raising the possibility of direct coupling of respiration to antiport-dependent pH homeostasis. This study characterized a homologous type II NADH dehydrogenase of genetically tractable alkaliphilic Bacillus pseudofirmus OF4, in which evidence supports antiport-based pH homeostasis that is mediated entirely by secondary antiport. Two candidate type II NADH dehydrogenase genes with canonical GXGXXG motifs were identified in a draft genome sequence of B. pseudofirmus OF4. The gene product designated NDH-2A exhibited homology to enzymes from Bacillus subtilis and Escherichia coli whereas NDH-2B exhibited homology to the H. dabanensis Nap protein and its alkaliphilic Bacillus halodurans C-125 homologue. The ndh-2A, but not the ndh-2B, gene complemented the growth defect of an NADH dehydrogenase-deficient E. coli mutant. Neither gene conferred Na+-resistance on an antiporter-deficient E. coli strain, nor did they confer Na+/H+ antiport activity in vesicle assays. The purified hexa-histidine-tagged gene products were approximately 50 kDa, contained noncovalently bound FAD and oxidized NADH. They were predominantly cytoplasmic in E. coli, consonant with the absence of antiport activity. The catalytic properties of NDH-2A were more consistent with a major respiratory role than those of NDH-2B.
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