Evidence map›Paper›PMID 11695827›Full record

ReviewJournal of bioenergetics and biomembranes2001

The Na+-translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: implications for the mechanism of redox-driven cation translocation by complex I.

J Steuber

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Sodium ion cycling mediates energy coupling between complex I and ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  4. 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

1 author.

J SteuberMikrobiologisches Institut der Eidgenössischen Technishen Hochschule, Zurich, Switzerland. steuber@micro.biol.ethz.ch

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic complex I integrated into the respiratory chain transports at least 4 H+ per NADH oxidized. Recent results indicate that the cation selectivity is altered to Na+ in complex I (NDH I) isolated from the enterobacteria Escherichia coli and Klebsiella pneumoniae. A sequence analysis illustrates the characteristic differences of the enterobacterial, Na+-translocating NDH I compared to the H+-translocating complex I from mitochondria. Special attention is given to the membranous NuoL (ND5, Nqo12) subunits that possess striking sequence similarities to secondary Na+/H+ antiporters and are proposed to participate in Na+ transport. A model of redox-linked Na+ (or H+) transport by complex I is discussed based on the ion-pair formation of a negatively charged ubisemiquinone anion with a positively charged Na+ (or H+).

Indexed as

Amino Acid SequenceElectron TransportElectron Transport Complex IEscherichia coliGenes, BacterialIon TransportKlebsiella pneumoniaeModels, BiologicalMolecular Sequence DataNADH, NADPH OxidoreductasesOperonOxidation-ReductionProtein SubunitsSequence Homology, Amino AcidSodiumSodium-Hydrogen ExchangersElectron Transport Complex INADH, NADPH OxidoreductasesProtein SubunitsSodiumSodium-Hydrogen Exchangers

Identifiers

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.