Evidence map›Paper›PMID 34409988›Full record

ArticleThe Biochemical journal2021

Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.

Sven T Stripp, Jonathan Oltmanns, Christina S Müller, David Ehrenberg, Ramona Schlesinger, Joachim Heberle, Lorenz Adrian, Volker Schünemann, Antonio J Pierik, Basem Soboh

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 47% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. ATP-Triggered Fe(CN)Journal of the American Chemical Society · 2024
    Article
  2. Article
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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

10 authors at 3 institutions in 1 country.

Sven T StrippExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany.ORCID 0000-0002-8412-0258
Jonathan OltmannsBiophysics and Medical Physics, Department of Physics, Technische Universität Kaiserslautern, Erwin-Schrödinger-Straße 56, 67663 Kaiserslautern, Germany.
Christina S MüllerBiophysics and Medical Physics, Department of Physics, Technische Universität Kaiserslautern, Erwin-Schrödinger-Straße 56, 67663 Kaiserslautern, Germany.
David EhrenbergExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany.
Ramona SchlesingerGenetic Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany.
Joachim HeberleExperimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany.
Lorenz AdrianDepartment of Environmental Biotechnology, Helmholtz Centre for Environmental Research - UFZ, Permoserstraße 15, 04318 Leipzig, Germany.
Volker SchünemannBiophysics and Medical Physics, Department of Physics, Technische Universität Kaiserslautern, Erwin-Schrödinger-Straße 56, 67663 Kaiserslautern, Germany.
Antonio J PierikBiochemistry, Department of Chemistry, Technische Universität Kaiserslautern, Erwin-Schrödinger-Straße 54, 67663 Kaiserslautern, Germany.
Basem SobohGenetic Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany.ORCID 0000-0002-1115-326X
Freie Universität Berlin · DEUniversity of Kaiserslautern · DEHelmholtz Centre for Environmental Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The [4Fe-4S] cluster containing scaffold complex HypCD is the central construction site for the assembly of the [Fe](CN)2CO cofactor precursor of [NiFe]-hydrogenase. While the importance of the HypCD complex is well established, not much is known about the mechanism by which the CN- and CO ligands are transferred and attached to the iron ion. We report an efficient expression and purification system producing the HypCD complex from E. coli with complete metal content. This enabled in-depth spectroscopic characterizations. The results obtained by EPR and Mössbauer spectroscopy demonstrate that the [Fe](CN)2CO cofactor and the [4Fe-4S] cluster of the HypCD complex are redox active. The data indicate a potential-dependent interconversion of the [Fe]2+/3+ and [4Fe-4S]2+/+ couple, respectively. Moreover, ATR FTIR spectroscopy reveals potential-dependent disulfide formation, which hints at an electron confurcation step between the metal centers. MicroScale thermophoresis indicates preferable binding between the HypCD complex and its in vivo interaction partner HypE under reducing conditions. Together, these results provide comprehensive evidence for an electron inventory fit to drive multi-electron redox reactions required for the assembly of the CN- and CO ligands on the scaffold complex HypCD.

Indexed as

Carbon MonoxideCatalytic DomainDisulfidesElectronsElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsHydrogenaseIonsIronIron-Sulfur ProteinsLigandsOxidation-ReductionProtein BindingProteinsSpectroscopy, Fourier Transform InfraredCarbon MonoxideDisulfidesEscherichia coli ProteinsHydrogenaseHypC protein, E coliHypD protein, BacteriaHypE protein, E coliIonsIronIron-Sulfur ProteinsLigandsnickel-iron hydrogenaseProteinsSulfurbiosynthesiscarbon monoxidecyanideFe-S proteinsmaturationredox activity

Identifiers

PMID34409988
PMCPMC8454700
OpenAlexW3195761187

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.