Evidence map›Paper›PMID 25258081›Full record

ArticleScience (New York, N.Y.)2014

Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase.

Thomas Spatzal, Kathryn A Perez, Oliver Einsle, James B Howard, Douglas C Rees

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.

0numbers the graph read from it
0cells of the map it votes in
158citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

158 citing papers in PubMed, 403 citations in OpenAlex.

  1. Article
  2. Molecular basis of NNature communications · 2026
    Article
  3. Article
  4. A Proposed Complete-Cycle Mechanism for Conversion of NChembiochem : a European journal of chemical biology · 2026
    Article
  5. Reversible NNational science review · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Synthetic models of the nitrogenase FeMo cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. The nitrogenase mechanism: new roles for the dangler?Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

98 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Thomas SpatzalHoward Hughes Medical Institute and Division of Chemistry and Chemical Engineering, MailCode 114-96, California Institute of Technology, Pasadena, CA 91125, USA. spatzal@caltech.edu dcrees@caltech.edu.
Kathryn A PerezHoward Hughes Medical Institute and Division of Chemistry and Chemical Engineering, MailCode 114-96, California Institute of Technology, Pasadena, CA 91125, USA.
Oliver EinsleInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, 79104 Freiburg, Germany. BIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-Universität Freiburg, 79104 Freiburg, Germany.
James B HowardHoward Hughes Medical Institute and Division of Chemistry and Chemical Engineering, MailCode 114-96, California Institute of Technology, Pasadena, CA 91125, USA. Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Douglas C ReesHoward Hughes Medical Institute and Division of Chemistry and Chemical Engineering, MailCode 114-96, California Institute of Technology, Pasadena, CA 91125, USA. spatzal@caltech.edu dcrees@caltech.edu.
University of Freiburg · DEUniversity of Minnesota · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI REESE, MICHAEL LLOYD · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
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
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIGMS NIH HHS GM45162NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM045162NIGMS NIH HHS R37 GM045162
6 · The paper itself

Abstract

The mechanism of nitrogenase remains enigmatic, with a major unresolved issue concerning how inhibitors and substrates bind to the active site. We report a crystal structure of carbon monoxide (CO)-inhibited nitrogenase molybdenum-iron (MoFe)-protein at 1.50 angstrom resolution, which reveals a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor. The μ2 binding geometry is achieved by replacing a belt-sulfur atom (S2B) and highlights the generation of a reactive iron species uncovered by the displacement of sulfur. The CO inhibition is fully reversible as established by regain of enzyme activity and reappearance of S2B in the 1.43 angstrom resolution structure of the reactivated enzyme. The substantial and reversible reorganization of the FeMo-cofactor accompanying CO binding was unanticipated and provides insights into a catalytically competent state of nitrogenase.

Indexed as

Nitrogen FixationCarbon MonoxideCatalytic DomainCrystallography, X-RayEnzyme ActivationLigandsMolybdoferredoxinProtein BindingSulfurCarbon MonoxideLigandsMolybdoferredoxinSulfur

Identifiers

PMID25258081
PMCPMC4205161
OpenAlexW2089422561

What OpenQuestion holds

Textmetadata
LicenceTDM
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.