ReviewMetal ions in life sciences2015
Production of dioxygen in the dark: dismutases of oxyanions.
Review in Metal ions in life sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Unique Biradical Intermediate in the Mechanism of the Heme Enzyme Chlorite Dismutase.ACS catalysis · 2021Article
- Effect of Chlorination on Microbiological Quality of Effluent of a Full-Scale Wastewater Treatment Plant.Life (Basel, Switzerland) · 2021Article
- Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020Article
- Distinguishing Active Site Characteristics of Chlorite Dismutases with Their Cyanide Complexes.Biochemistry · 2018Article
- Microbial Synthesis and Transformation of Inorganic and Organic Chlorine Compounds.Frontiers in microbiology · 2018Review
- Active Sites of OBiochemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
O₂-generating reactions are exceedingly rare in biology and difficult to mimic synthetically. Perchlorate-respiring bacteria enzymatically detoxify chlorite (ClO₂(-) ), the end product of the perchlorate (ClO(4)(-) ) respiratory pathway, by rapidly converting it to dioxygen (O₂) and chloride (Cl(-)). This reaction is catalyzed by a heme-containing protein, called chlorite dismutase (Cld), which bears no structural or sequence relationships with known peroxidases or other heme proteins and is part of a large family of proteins with more than one biochemical function. The original assumptions from the 1990s that perchlorate is not a natural product and that perchlorate respiration might be confined to a taxonomically narrow group of species have been called into question, as have the roles of perchlorate respiration and Cld-mediated reactions in the global biogeochemical cycle of chlorine. In this chapter, the chemistry and biochemistry of Cld-mediated O₂generation, as well as the biological and geochemical context of this extraordinary reaction, are described.
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What OpenQuestion holds
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.