Evidence map›Paper›PMID 38740794›Full record

ArticleNature communications2024

Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra.

Lorenz Heidinger, Kathryn Perez, Thomas Spatzal, Oliver Einsle, Stefan Weber, Douglas C Rees, Erik Schleicher

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Nature communications · 2025
    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

7 authors.

Lorenz HeidingerInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Kathryn PerezHoward Hughes Medical Institute (HHMI), California Institute of Technology, Division of Chemistry and Chemical Engineering, Pasadena, CA, USA.
Thomas SpatzalHoward Hughes Medical Institute (HHMI), California Institute of Technology, Division of Chemistry and Chemical Engineering, Pasadena, CA, USA.
Oliver EinsleInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Stefan WeberInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.ORCID http://orcid.org/0000-0003-4090-7435
Douglas C ReesHoward Hughes Medical Institute (HHMI), California Institute of Technology, Division of Chemistry and Chemical Engineering, Pasadena, CA, USA. dcrees@caltech.edu.ORCID http://orcid.org/0000-0003-4073-1185
Erik SchleicherInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany. erik.schleicher@pc.uni-freiburg.de.ORCID http://orcid.org/0000-0003-3010-9528

Funding

Crystallographic Studies of Electron Tranfer ProteinsR37GM045162 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI REES, DOUGLAS CHARLES · 2003 to 2012
$3.1M
CRYSTALLOGRAPHIC STUDIES OF ELECTRON TRANSFER PROTEINSR01GM045162 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI REES, DOUGLAS CHARLES · 1991 to 2018
$2.2M
Deutsche Forschungsgemeinschaft (German Research Foundation) ID 235777276Deutsche Forschungsgemeinschaft (German Research Foundation) ID311061829NIGMS NIH HHS R01 GM045162NIGMS NIH HHS R37 GM045162U.S. Department of Health & Human Services | NIH | Center for Information Technology (Center for Information Technology, National Institutes of Health) GM045162
6 · The paper itself

Abstract

Due to the complexity of the catalytic FeMo cofactor site in nitrogenases that mediates the reduction of molecular nitrogen to ammonium, mechanistic details of this reaction remain under debate. In this study, selenium- and sulfur-incorporated FeMo cofactors of the catalytic MoFe protein component from Azotobacter vinelandii are prepared under turnover conditions and investigated by using different EPR methods. Complex signal patterns are observed in the continuous wave EPR spectra of selenium-incorporated samples, which are analyzed by Tikhonov regularization, a method that has not yet been applied to high spin systems of transition metal cofactors, and by an already established grid-of-error approach. Both methods yield similar probability distributions that reveal the presence of at least four other species with different electronic structures in addition to the ground state E

Indexed as

Azotobacter vinelandiiMolybdoferredoxinNitrogenaseSeleniumSulfurBacterial ProteinsElectron Spin Resonance SpectroscopyBacterial ProteinsMolybdoferredoxinNitrogenaseSeleniumSulfur

Identifiers

PMID38740794
PMCPMC11091149

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Registered trials

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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.