Evidence map›Paper›PMID 23857587›Full record

ArticleThe Journal of biological chemistry2013

Characterization of a nitrite reductase involved in nitrifier denitrification.

Thomas J Lawton, Kimberly E Bowen, Luis A Sayavedra-Soto, Daniel J Arp, Amy C Rosenzweig

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 15% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 48 citations in OpenAlex.

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  13. The Rise of Radicals in Bioinorganic Chemistry.Israel journal of chemistry · 2016
    Article
  14. Article
  15. Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Thomas J LawtonFrom the Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208 and.
Kimberly E BowenFrom the Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208 and.
Luis A Sayavedra-SotoDepartment of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331.
Daniel J ArpDepartment of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331.
Amy C RosenzweigFrom the Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208 and. Electronic address: amyr@northwestern.edu.
Northwestern University · USOregon State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrifier denitrification is the conversion of nitrite to nitrous oxide by ammonia-oxidizing organisms. This process, which is distinct from denitrification, is active under aerobic conditions in the model nitrifier Nitrosomonas europaea. The central enzyme of the nitrifier dentrification pathway is a copper nitrite reductase (CuNIR). To understand how a CuNIR, typically inactivated by oxygen, functions in this pathway, the enzyme isolated directly from N. europaea (NeNIR) was biochemically and structurally characterized. NeNIR reduces nitrite at a similar rate to other CuNIRs but appears to be oxygen tolerant. Crystal structures of oxidized and reduced NeNIR reveal a substrate channel to the active site that is much more restricted than channels in typical CuNIRs. In addition, there is a second fully hydrated channel leading to the active site that likely acts a water exit pathway. The structure is minimally affected by changes in pH. Taken together, these findings provide insight into the molecular basis for NeNIR oxygen tolerance.

Indexed as

Bacterial ProteinsCatalytic DomainCrystallography, X-RayDenitrificationNitrite ReductasesNitritesNitrosomonas europaeaOxidation-ReductionOxygenBacterial ProteinsNitrite ReductasesNitritesOxygenCopperCrystal StructureDenitrificationElectron TransferNitrifierNitrite ReductaseNitrogen MetabolismNitrosomonas europaeaOxygen Binding

Identifiers

PMID23857587
PMCPMC3757218
OpenAlexW1976654009

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.