ArticleThe Biochemical journal2007
A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 69 citations in OpenAlex.
- Structural basis of Neisseria meningitidis quinol dependent nitric oxide reductase activation by dimerization.Communications biology · 2026Article
- Insertion of the FeFEBS letters · 2025Article
- Preparation for Denitrification and Phenotypic Diversification at the Cusp of Anoxia: a Purpose for NApplied and environmental microbiology · 2022Article
- Incomplete denitrification phenotypes in diverse Thermus species from diverse geothermal spring sediments and adjacent soils in southwest China.Extremophiles : life under extreme conditions · 2022Article
- Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.Chemical reviews · 2020Review
- Functional interactions between nitrite reductase and nitric oxide reductase from Paracoccus denitrificans.Scientific reports · 2019Article
- Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy.Science advances · 2019Article
- Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.Scientific reports · 2018Article
- Periplasmic Nicotine Dehydrogenase NdhAB Utilizes Pseudoazurin as Its Physiological Electron Acceptor in Agrobacterium tumefaciens S33.Applied and environmental microbiology · 2017Article
- Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Israel journal of chemistry · 2016Article
- Insights into the structure and function of HV1 from a meta-analysis of mutation studies.The Journal of general physiology · 2016Review
- Article
- The nitric-oxide reductase from Paracoccus denitrificans uses a single specific proton pathway.The Journal of biological chemistry · 2013Article
- Characterization of the nitric oxide reductase from Thermus thermophilus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Structural basis for nitrous oxide generation by bacterial nitric oxide reductases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Article
- Bacterial adaptation of respiration from oxic to microoxic and anoxic conditions: redox control.Antioxidants & redox signaling · 2012Review
- Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus.Nature structural & molecular biology · 2012Article
- Molecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductase.PLoS computational biology · 2012Article
- Bacterial oxygen production in the dark.Frontiers in microbiology · 2012Article
Corrections and comments
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4 authors at 1 institution in 1 country.
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Abstract
A specific amperometric assay was developed for the membrane-bound NOR [NO (nitric oxide) reductase] from the model denitrifying bacterium Paracoccus denitrificans using its natural electron donor, pseudoazurin, as a co-substrate. The method allows the rapid and specific assay of NO reduction catalysed by recombinant NOR expressed in the cytoplasmic membranes of Escherichia coli. The effect on enzyme activity of substituting alanine, aspartate or glutamine for two highly conserved glutamate residues, which lie in a periplasmic facing loop between transmembrane helices III and IV in the catalytic subunit of NOR, was determined using this method. Three of the substitutions (E122A, E125A and E125D) lead to an almost complete loss of NOR activity. Some activity is retained when either Glu122 or Glu125 is substituted with a glutamine residue, but only replacement of Glu122 with an aspartate residue retains a high level of activity. These results are interpreted in terms of these residues forming the mouth of a channel that conducts substrate protons to the active site of NOR during turnover. This channel is also likely to be that responsible in the coupling of proton movement to electron transfer during the oxidation of fully reduced NOR with oxygen [U. Flock, N. J. Watmough and P. Adelroth (2005) Biochemistry 44, 10711-10719].
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