Evidence map›Paper›PMID 28801050›Full record

ArticleBiochimica et biophysica acta. Bioenergetics2017

Electron transfer through arsenite oxidase: Insights into Rieske interaction with cytochrome c.

Cameron Watson, Dimitri Niks, Russ Hille, Marta Vieira, Barbara Schoepp-Cothenet, Alexandra T Marques, Maria João Romão, Teresa Santos-Silva, Joanne M Santini

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Bioenergetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 21 citations in OpenAlex.

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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

9 authors at 6 institutions in 4 countries.

Cameron WatsonInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, WC1E 6BT, United Kingdom.
Dimitri NiksDepartment of Biochemistry, University of California; Riverside, Riverside, CA 92521, USA.
Russ HilleDepartment of Biochemistry, University of California; Riverside, Riverside, CA 92521, USA.
Marta VieiraUCIBIO-Requimte, Department of Chemistry, Faculty of Sciences and Technology, Universidade Nova de Lisboa, Portugal.
Barbara Schoepp-CothenetAix-Marseille Univ, CNRS, BIP UMR 7281, 31 chemin J. Aiguier, 13402 Marseille Cedex 20, France.
Alexandra T MarquesUCIBIO-Requimte, Department of Chemistry, Faculty of Sciences and Technology, Universidade Nova de Lisboa, Portugal.
Maria João RomãoUCIBIO-Requimte, Department of Chemistry, Faculty of Sciences and Technology, Universidade Nova de Lisboa, Portugal.
Teresa Santos-SilvaUCIBIO-Requimte, Department of Chemistry, Faculty of Sciences and Technology, Universidade Nova de Lisboa, Portugal.
Joanne M SantiniInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, WC1E 6BT, United Kingdom. Electronic address: j.santini@ucl.ac.uk.
Universidade Nova de Lisboa · PTUniversity of California, Riverside · USAix-Marseille Université · FRInstitute of Structural and Molecular Biology · GBUnidade em Ciências Biomoleculares AplicadasUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arsenic is a widely distributed environmental toxin whose presence in drinking water poses a threat to >140 million people worldwide. The respiratory enzyme arsenite oxidase from various bacteria catalyses the oxidation of arsenite to arsenate and is being developed as a biosensor for arsenite. The arsenite oxidase from Rhizobium sp. str. NT-26 (a member of the Alphaproteobacteria) is a heterotetramer consisting of a large catalytic subunit (AioA), which contains a molybdenum centre and a 3Fe-4S cluster, and a small subunit (AioB) containing a Rieske 2Fe-2S cluster. Stopped-flow spectroscopy and isothermal titration calorimetry (ITC) have been used to better understand electron transfer through the redox-active centres of the enzyme, which is essential for biosensor development. Results show that oxidation of arsenite at the active site is extremely fast with a rate of >4000s

Indexed as

ArsenitesBetaproteobacteriaCatalysisCatalytic DomainCytochromes cElectronsElectron TransportMolybdenumOxidation-ReductionOxidoreductasesProtein Interaction MapsProtein Subunitsarsenitearsenite oxidaseArsenitesCytochromes cMolybdenumOxidoreductasesProtein SubunitsArsenite oxidaseCytochrome cIsothermal titration calorimetryMolybdenum enzymeRate-limiting stepRieske proteinStopped-flow spectroscopy

Identifiers

PMID28801050
PMCPMC5574378
OpenAlexW2742867937

What OpenQuestion holds

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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.