Evidence map›Paper›PMID 25268953›Full record

ReviewBiochimica et biophysica acta2015

The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.

Kenichi Yokoyama, Silke Leimkühler

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. 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
1.0field-weighted citation impact, top 24% 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, 39 citations in OpenAlex.

  1. Review
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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

2 authors at 2 institutions in 2 countries.

Kenichi YokoyamaDepartment of Biochemistry, Duke University Medical Center, Durham, NC, USA.
Silke LeimkühlerDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany. Electronic address: sleim@uni-potsdam.de.
Duke University · USUniversity of Potsdam · DE

Funding

Mechanism of cofactor biosynthesis required for chronic bacterial infectionR01GM112838 · NIGMS · DUKE UNIVERSITY · PI YOKOYAMA, KENICHI · 2015 to 2023
$2.8M
NIGMS NIH HHS R01 GM112838
6 · The paper itself

Abstract

The biosynthesis of the molybdenum cofactor (Moco) has been intensively studied, in addition to its insertion into molybdoenzymes. In particular, a link between the assembly of molybdoenzymes and the biosynthesis of FeS clusters has been identified in the recent years: 1) the synthesis of the first intermediate in Moco biosynthesis requires an FeS-cluster containing protein, 2) the sulfurtransferase for the dithiolene group in Moco is also involved in the synthesis of FeS clusters, thiamin and thiolated tRNAs, 3) the addition of a sulfido-ligand to the molybdenum atom in the active site additionally involves a sulfurtransferase, and 4) most molybdoenzymes in bacteria require FeS clusters as redox active cofactors. In this review we will focus on the biosynthesis of the molybdenum cofactor in bacteria, its modification and insertion into molybdoenzymes, with an emphasis to its link to FeS cluster biosynthesis and sulfur transfer.

Indexed as

BacteriaBacterial ProteinsCoenzymesIron-Sulfur ProteinsMetalloproteinsModels, BiologicalModels, ChemicalMolecular StructureMolybdenumMolybdenum CofactorsOxidoreductasesPteridinesBacterial ProteinsCoenzymesIron-Sulfur ProteinsMetalloproteinsMolybdenumMolybdenum CofactorsmolybdopterinOxidoreductasesPteridinesl-Cysteine desulfuraseMolybdenum cofactorMolybdenum–iron–iron–sulfur clusterSulfur transfertRNA

Identifiers

PMID25268953
PMCPMC4834969
OpenAlexW2025902660

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.