Evidence map›Paper›PMID 20925337›Full record

ArticleJournal of the American Chemical Society2010

Hydride-containing models for the active site of the nickel-iron hydrogenases.

Bryan E Barton, Thomas B Rauchfuss

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
8.5field-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

37 citing papers in PubMed, 234 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Hybrids of [FeFe]- and [NiFe]-HOrganometallics · 2023
    Article
  5. Article
  6. Article
  7. Electronic Structure andNanomaterials (Basel, Switzerland) · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Modular bimetallic complexes with a sulfonamido-based ligand.Dalton transactions (Cambridge, England : 2003) · 2018
    Article
  14. Article
  15. Interplay of hemilability and redox activity in models of hydrogenase active sites.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Bryan E BartonSchool of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Thomas B Rauchfuss
University 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 R01 GM061153
6 · The paper itself

Abstract

The [NiFe]-hydrogenase model complex NiFe(pdt)(dppe)(CO)(3) (1) (pdt = 1,3-propanedithiolate) has been efficiently synthesized and found to be robust. This neutral complex sustains protonation to give the first nickel-iron hydride [1H]BF(4). One CO ligand in [1H]BF(4) is readily substituted by organophosphorus ligands to afford the substituted derivatives [HNiFe(pdt)(dppe)(PR(3))(CO)(2)]BF(4), where PR(3) = P(OPh)(3) ([2H]BF(4)); PPh(3) ([3H]BF(4)); PPh(2)Py ([4H]BF(4), where Py = 2-pyridyl). Variable temperature NMR measurements show that the neutral and protonated derivatives are dynamic on the NMR time scale, which partially symmetrizes the phosphine complex. The proposed stereodynamics involve twisting of the Ni(dppe) center, not rotation at the Fe(CO)(2)(PR(3)) center. In MeCN solution, 3, which can be prepared by deprotonation of [3H]BF(4) with NaOMe, is about 10(4) stronger base than is 1. X-ray crystallographic analysis of [3H]BF(4) revealed a highly unsymmetrical bridging hydride, the Fe-H bond being 0.40 Å shorter than the Ni-H distance. Complexes [2H]BF(4), [3H]BF(4), and [4H]BF(4) undergo reductions near -1.46 V vs Fc(0/+). For [2H]BF(4), this reduction process is reversible, and we assign it as a one-electron process. In the presence of trifluoroacetic acid, proton reduction catalysis coincides with this reductive event. The dependence of i(c)/i(p) on the concentration of the acid indicates that H(2) evolution entails protonation of a reduced hydride. For [2H](+), [3H](+), and [4H](+), the acid-independent rate constants are 50-75 s(-1). For [2H](+) and [3H](+), the overpotentials for H(2) evolution are estimated to be 430 mV, whereas the overpotential for the N-protonated pyridinium complex [4H(2)](2+) is estimated to be 260 mV. The mechanism of H(2) evolution is proposed to follow an ECEC sequence, where E and C correspond to one-electron reductions and protonations, respectively. On the basis of their values for its pK(a) and redox potentials, the room temperature values of ΔG(H•) and ΔG(H-) are estimated as respectively as 57 and 79 kcal/mol for [1H](+).

Indexed as

Models, ChemicalCatalysisCatalytic DomainCrystallography, X-RayHydrogenHydrogenaseModels, MolecularNuclear Magnetic Resonance, BiomolecularSpectroscopy, Fourier Transform InfraredHydrogenHydrogenasenickel-iron hydrogenase

Identifiers

PMID20925337
PMCPMC2980840
OpenAlexW1995497527

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.