Evidence map›Paper›PMID 25645603›Full record

ArticleAngewandte Chemie (International ed. in English)2015

Hydrogen-bonding interactions trigger a spin-flip in iron(III) porphyrin complexes.

Dipankar Sahoo, Matthew G Quesne, Sam P de Visser, Sankar Prasad Rath

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Heme-copper and Heme OJournal of inorganic biochemistry · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. All high-spin (S = 2) iron(ii) hemes are NOT alike.Dalton transactions (Cambridge, England : 2003) · 2015
    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

4 authors.

Dipankar SahooDepartment of Chemistry, Indian Institute of Technology Kanpur, Kanpur-208016 (India).
Matthew G Quesne
Sam P de Visser
Sankar Prasad Rath

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

A key step in cytochrome P450 catalysis includes the spin-state crossing from low spin to high spin upon substrate binding and subsequent reduction of the heme. Clearly, a weak perturbation in P450 enzymes triggers a spin-state crossing. However, the origin of the process whereby enzymes reorganize their active site through external perturbations, such as hydrogen bonding, is still poorly understood. We have thus studied the impact of hydrogen-bonding interactions on the electronic structure of a five-coordinate iron(III) octaethyltetraarylporphyrin chloride. The spin state of the metal was found to switch reversibly between high (S=5/2) and intermediate spin (S=3/2) with hydrogen bonding. Our study highlights the possible effects and importance of hydrogen-bonding interactions in heme proteins. This is the first example of a synthetic iron(III) complex that can reversibly change its spin state between a high and an intermediate state through weak external perturbations.

Indexed as

Cytochrome P-450 Enzyme SystemFerric CompoundsHydrogen BondingMolecular ConformationPorphyrinsQuantum TheorySpectroscopy, MossbauerThermodynamicsCytochrome P-450 Enzyme SystemFerric CompoundsPorphyrinselectronic structurehydrogen bondingporphyrinoidsspin crossoverstructure elucidation

Identifiers

PMID25645603
PMCPMC4687417

What OpenQuestion holds

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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.