Evidence map›Paper›PMID 28067272›Full record

ArticleScientific reports2017

The mechanism of catalysis by type-II NADH:quinone oxidoreductases.

James N Blaza, Hannah R Bridges, David Aragão, Elyse A Dunn, Adam Heikal, Gregory M Cook, Yoshio Nakatani, Judy Hirst

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 71 citations in OpenAlex.

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  12. Reactions ofInternational journal of molecular sciences · 2025
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  14. Effect of Light Regime onJournal of microbiology and biotechnology · 2024
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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

8 authors at 5 institutions in 3 countries.

James N BlazaMRC Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.
Hannah R BridgesMRC Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.
David AragãoAustralian Synchrotron, 800 Blackburn Road, Clayton, Victoria VIC3168, Australia.
Elyse A DunnDepartment of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand.
Adam HeikalDepartment of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand.
Gregory M CookDepartment of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand.
Yoshio NakataniDepartment of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand.
Judy HirstMRC Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.
MRC Mitochondrial Biology Unit · GBUniversity of Auckland · NZUniversity of Otago · NZAustralian Synchrotron · AUWellcome Trust · GB

Funding

Medical Research Council MC_U105663141Medical Research Council MC_UU_00015/2Medical Research Council MC_UU_00015/7
6 · The paper itself

Abstract

Type II NADH:quinone oxidoreductase (NDH-2) is central to the respiratory chains of many organisms. It is not present in mammals so may be exploited as an antimicrobial drug target or used as a substitute for dysfunctional respiratory complex I in neuromuscular disorders. NDH-2 is a single-subunit monotopic membrane protein with just a flavin cofactor, yet no consensus exists on its mechanism. Here, we use steady-state and pre-steady-state kinetics combined with mutagenesis and structural studies to determine the mechanism of NDH-2 from Caldalkalibacillus thermarum. We show that the two substrate reactions occur independently, at different sites, and regardless of the occupancy of the partner site. We conclude that the reaction pathway is determined stochastically, by the substrate/product concentrations and dissociation constants, and can follow either a ping-pong or ternary mechanism. This mechanistic versatility provides a unified explanation for all extant data and a new foundation for the development of therapeutic strategies.

Indexed as

CatalysisBacillalesBinding SitesDinitrocresolsKineticsProtein BindingQuinone ReductasesReactive Oxygen Species4,6-dinitro-o-cresolDinitrocresolsNADH dehydrogenase (quinone)Quinone ReductasesReactive Oxygen Species

Identifiers

PMID28067272
PMCPMC5220320
OpenAlexW2571059898

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.