Evidence map›Paper›PMID 22800196›Full record

ArticleInorganic chemistry2012

EPR/ENDOR, Mössbauer, and quantum-chemical investigations of diiron complexes mimicking the active oxidized state of [FeFe]hydrogenase.

Alexey Silakov, Matthew T Olsen, Stephen Sproules, Eduard J Reijerse, Thomas B Rauchfuss, Wolfgang Lubitz

Abstract read
In one paragraph

Article in Inorganic chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

6 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. 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

6 authors at 2 institutions in 2 countries.

Alexey SilakovMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, Mülheim a.d. Ruhr 45470, Germany. aus40@psu.edu
Matthew T Olsen
Stephen Sproules
Eduard J Reijerse
Thomas B Rauchfuss
Wolfgang Lubitz
Max Planck Institute for Chemical Energy Conversion · DEUniversity of Illinois Urbana-Champaign · US

Funding

FE-S ENSEMBLES RELATED TO HYDROGENASE ACTIVITYR01GM061153 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RAUCHFUSS, THOMAS · 2000 to 2025
$6.7M
NIGMS NIH HHS GM061153NIGMS NIH HHS R01 GM061153
6 · The paper itself

Abstract

Understanding the catalytic process of the heterolytic splitting and formation of molecular hydrogen is one of the key topics for the development of a future hydrogen economy. With an interest in elucidating the enzymatic mechanism of the [Fe(2)(S(2)C(2)H(4)NH)(CN)(2)(CO)(2)(μ-CO)] active center uniquely found in [FeFe]hydrogenases, we present a detailed spectroscopic and theoretical analysis of its inorganic model [Fe(2)(S(2)X)(CO)(3)(dppv)(PMe(3))](+) [dppv = cis-1,2-bis(diphenylphosphino)ethylene] in two forms with S(2)X = ethanedithiolate (1edt) and azadithiolate (1adt). These complexes represent models for the oxidized mixed-valent Fe(I)Fe(II) state analogous to the active oxidized "H(ox)" state of the native H-cluster. For both complexes, the (31)P hyperfine interactions were determined by pulse electron paramagnetic resonance and electron nuclear double resonance (ENDOR) methods. For 1edt, the (57)Fe parameters were measured by electron spin-echo envelope modulation and Mössbauer spectroscopy, while for 1adt, (14)N and selected (1)H couplings could be obtained by ENDOR and hyperfine sublevel correlation spectroscopy. The spin density was found to be predominantly localized on the Fe(dppv) site. This spin distribution is different from that of the H-cluster, where both the spin and charge densities are delocalized over the two Fe centers. This difference is attributed to the influence of the "native" cubane subcluster that is lacking in the inorganic models. The degree and character of the unpaired spin delocalization was found to vary from 1edt, with an abiological dithiolate, to 1adt, which features the authentic cofactor. For 1adt, we find two (14)N signals, which are indicative for two possible isomers of the azadithiolate, demonstrating its high flexibility. All interaction parameters were also evaluated through density functional theory calculations at various levels.

Indexed as

ElectronsBinding SitesBiomimetic MaterialsCatalysisCrystallography, X-RayElectron Spin Resonance SpectroscopyFerrous CompoundsHydrogenHydrogenaseIron-Sulfur ProteinsModels, MolecularOrganometallic CompoundsOxidation-ReductionQuantum TheorySpectroscopy, MossbauerStereoisomerismFerrous CompoundsHydrogenHydrogenaseIron-Sulfur ProteinsOrganometallic CompoundsSulfhydryl Compounds

Identifiers

PMID22800196
PMCPMC3420818
OpenAlexW2077159053

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.