ArticleFree radical biology & medicine2015
Observation of superoxide production during catalysis of Bacillus subtilis oxalate decarboxylase at pH 4.
Article in Free radical biology & medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Bidentate Substrate Binding Mode in Oxalate Decarboxylase.Molecules (Basel, Switzerland) · 2024Article
- Oxalic acid degradation in wood-rotting fungi. Searching for a new source of oxalate oxidase.World journal of microbiology & biotechnology · 2022Article
- Oxalate decarboxylase uses electron hole hopping for catalysis.The Journal of biological chemistry · 2021Article
- On the modeling of amplitude-sensitive electron spin resonance (ESR) detection using voltage-controlled oscillator (VCO)-based ESR-on-a-chip detectors.Magnetic resonance (Gottingen, Germany) · 2021Article
- Structural, Spectroscopic, Electrochemical, and Magnetic Properties for Manganese(II) Triazamacrocyclic Complexes.Inorganica chimica acta · 2019Article
- Oxygen activation by mononuclear Mn, Co, and Ni centers in biology and synthetic complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Hydrogen peroxide inhibition of bicupin oxalate oxidase.PloS one · 2017Article
- Substrate Binding Mode and Molecular Basis of a Specificity Switch in Oxalate Decarboxylase.Biochemistry · 2016Article
- Formation of Hexacoordinate Mn(III) in Bacillus subtilis Oxalate Decarboxylase Requires Catalytic Turnover.Biochemistry · 2016Article
- Immobilization ofBiochemistry and biophysics reports · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
This contribution describes the trapping of the hydroperoxyl radical at a pH of 4 during turnover of wild-type oxalate decarboxylase and its T165V mutant using the spin-trap BMPO. Radicals were detected and identified by a combination of EPR and mass spectrometry. Superoxide, or its conjugate acid, the hydroperoxyl radical, is expected as an intermediate in the decarboxylation and oxidation reactions of the oxalate monoanion, both of which are promoted by oxalate decarboxylase. Another intermediate, the carbon dioxide radical anion was also observed. The quantitative yields of superoxide trapping are similar in the wild type and the mutant while it is significantly different for the trapping of the carbon dioxide radical anion. This suggests that the two radicals are released from different sites of the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.