Evidence map›Paper›PMID 25710326›Full record

ArticleBiochemistry2015

Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.

Christine N Morrison, Julie A Hoy, Limei Zhang, Oliver Einsle, Douglas C Rees

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Near ambient NNature reviews. Chemistry · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Statistical analysis of PRSC advances · 2022
    Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Characterization of the Earliest Intermediate of Fe-NJournal of the American Chemical Society · 2019
    Article
  19. A Structural Basis forChemphyschem : a European journal of chemical physics and physical chemistry · 2019
    Article
  20. 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

5 authors at 2 institutions in 2 countries.

Christine N Morrison†Division of Chemistry and Chemical Engineering, California Institute of Technology 114-96, Pasadena, California 91125, United States.
Julie A Hoy†Division of Chemistry and Chemical Engineering, California Institute of Technology 114-96, Pasadena, California 91125, United States.
Limei Zhang†Division of Chemistry and Chemical Engineering, California Institute of Technology 114-96, Pasadena, California 91125, United States.
Oliver Einsle‡Institut für Biochemie and BIOSS Centre for Biological Signaling Studies, Albert-Ludwigs-Universität Freiburg, 79104 Freiburg, Germany.
Douglas C Rees†Division of Chemistry and Chemical Engineering, California Institute of Technology 114-96, Pasadena, California 91125, United States.
California Institute of Technology · USUniversity of Freiburg · DE

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 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
European Research Council 310656Howard Hughes Medical InstituteNCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIGMS NIH HHS GM45162NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM045162
6 · The paper itself

Abstract

In the nitrogenase molybdenum-iron (MoFe) protein, we have identified five potential substrate access pathways from the protein surface to the FeMo-cofactor (the active site) or the P-cluster using experimental structures of Xe pressurized into MoFe protein crystals from Azotobacter vinelandii and Clostridium pasteurianum. Additionally, all published structures of the MoFe protein, including those from Klebsiella pneumoniae, were analyzed for the presence of nonwater, small molecules bound to the protein interior. Each pathway is based on identification of plausible routes from buried small molecule binding sites to both the protein surface and a metallocluster. Of these five pathways, two have been previously suggested as substrate access pathways. While the small molecule binding sites are not conserved among the three species of MoFe protein, residues lining the pathways are generally conserved, indicating that the proposed pathways may be accessible in all three species. These observations imply that there is unlikely a unique pathway utilized for substrate access from the protein surface to the active site; however, there may be preferred pathways such as those described here.

Indexed as

Models, MolecularAmino Acid SequenceAzotobacter vinelandiiBacterial ProteinsBinding SitesCatalytic DomainClostridiumConserved SequenceCrystallography, X-RayKlebsiella pneumoniaeLigandsMolybdoferredoxinPressureProtein ConformationSurface PropertiesXenonBacterial ProteinsLigandsMolybdoferredoxinXenon

Identifiers

PMID25710326
PMCPMC4590346
OpenAlexW2116639266

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.