Evidence map›Paper›PMID 20485834›Full record

ReviewChemical Society reviews2010

Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes.

Simone Friedle, Erwin Reisner, Stephen J Lippard

Abstract readReview
In one paragraph

Review in Chemical Society reviews, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Review
  2. Review
  3. High-spin surface FeNature communications · 2025
    Article
  4. Review
  5. Metal-α-Helix Peptide Frameworks.Journal of the American Chemical Society · 2025
    Article
  6. Article
  7. Review
  8. 10Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Heteroleptic Ligation by an endo-Functionalized Cage.Angewandte Chemie (International ed. in English) · 2021
    Article
  14. Article
  15. Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers.Journal of the American Chemical Society · 2021
    Article
  16. Fate of model complexes with monocopper center towards the functional properties of type 2 and type 3 copper oxidases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  17. Opening the CoJournal of the American Chemical Society · 2020
    Article
  18. [BOAngewandte Chemie (International ed. in English) · 2020
    Article
  19. 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

3 authors.

Simone FriedleDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Erwin Reisner
Stephen J Lippard

Funding

NONHEME IRON AND THE BIOLOGICAL OXIDATION OF METHANER01GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J. · 1985 to 2013
$6.9M
LIGAND-BRIDGED POLYNUCLEAR METAL COMPLEXES &PROTEINSR37GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J · 1988 to 1997
–
NIGMS NIH HHS GM032134NIGMS NIH HHS R01 GM032134
6 · The paper itself

Abstract

This tutorial review describes recent progress in modeling the active sites of carboxylate-rich non-heme diiron enzymes that activate dioxygen to carry out several key reactions in Nature. The chemistry of soluble methane monooxygenase, which catalyzes the selective oxidation of methane to methanol, is of particular interest for (bio)technological applications. Novel synthetic diiron complexes that mimic structural, and, to a lesser extent, functional features of these diiron enzymes are discussed. The chemistry of the enzymes is also briefly summarized. A particular focus of this review is on models that mimic characteristics of the diiron systems that were previously not emphasized, including systems that contain (i) aqua ligands, (ii) different substrates tethered to the ligand framework, (iii) dendrimers attached to carboxylates to mimic the protein environment, (iv) two N-donors in a syn-orientation with respect to the iron-iron vector, and (v) a N-rich ligand environment capable of accessing oxygenated high-valent diiron intermediates.

Indexed as

Catalytic DomainIronModels, MolecularBiomimetic MaterialsEnzymesHumansOxygenEnzymesIronOxygen

Identifiers

PMID20485834
PMCPMC2909375

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.