Evidence map›Paper›PMID 9932647›Full record

ArticleJournal of bioenergetics and biomembranes1998

Studies of the electron transport chain of the euryarcheon Halobacterium salinarum: indications for a type II NADH dehydrogenase and a complex III analog.

K Sreeramulu, C L Schmidt, G Schäfer, S Anemüller

Abstract read
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In one paragraph

Article in Journal of bioenergetics and biomembranes, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-weighted citation impact, top 40% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Metabolism of halophilic archaea.Extremophiles : life under extreme conditions · 2008
    Review
  9. Article
  10. New insights into type II NAD(P)H:quinone oxidoreductases.Microbiology and molecular biology reviews : MMBR · 2004
    Review
  11. Article
  12. Cytochrome aa(3) in Haloferax volcanii.Journal of bacteriology · 2002
    Article
  13. Article
  14. Bioenergetics of the Archaea.Microbiology and molecular biology reviews : MMBR · 1999
    Review
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

4 authors at 1 institution in 1 country.

K SreeramuluDepartment of Biochemistry, Gulbarga University, India.
C L Schmidt
G Schäfer
S Anemüller
Gulbarga University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The components involved in the respiratory system of the euryarcheon Halobacterium salinarum were investigated by spectroscopic and polarographic techniques. Previous results about the cytochrome composition could be verified. However, under low oxygen tension, the expression of a d-type cytochrome was detected. Membranes exerted an NADH- and succinatecytochrome-c oxidoreductase as well as an NADH and succinate oxidase activity. These activities could be blocked by the following inhibitors: 7-jodocarboxylic acid, giving evidence for the presence of a type II NADH dehydrogenase, antimycin A, and myxothiazol, indicating the presence of a complex III analog, and the typical succinate dehydrogenase (SDH) and terminal oxidase inhibitors. Complex I inhibitors like rotenone and annonine were inactive, clearly excluding the presence of a coupled NADH dehydrogenase. In addition, no [Fe-S] resonances in the region of the NADH dehydrogenase (NDH) clusters could be observed after NADH addition. One of the terminal oxidases could be shown to act as a cytochrome-c oxidase with a Km value of 37 microM and an activation energy of 23.7 kJ/mol. The relative molecular mass of the endogenous c-type cytochrome could be determined as 14.1 kD. The complex III analog could be enriched after detergent extraction with Triton X-100 and hydroxylapatite (HTP) chromatography. The partially purified complex contained a Rieske iron-sulfur cluster, b- and c-type cytochromes, and was catalytically active in the decylubiquinone-cytochrome-c oxidoreductase assay.

Indexed as

Cytochrome d GroupElectron TransportElectron Transport Complex IIElectron Transport Complex IIIElectron Transport Complex IVHalobacteriumMultienzyme ComplexesNADH DehydrogenaseNAD(P)H Dehydrogenase (Quinone)OxidoreductasesOxygen ConsumptionSuccinate DehydrogenaseCytochrome d GroupElectron Transport Complex IIElectron Transport Complex IIIElectron Transport Complex IVMultienzyme ComplexesNADH DehydrogenaseNADH dehydrogenase IINAD(P)H Dehydrogenase (Quinone)OxidoreductasesSuccinate Dehydrogenase

Identifiers

PMID9932647
OpenAlexW285851164

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.