Evidence map›Paper›PMID 26079848›Full record

ArticleAccounts of chemical research2015

Diiron azadithiolates as models for the [FeFe]-hydrogenase active site and paradigm for the role of the second coordination sphere.

Thomas B Rauchfuss

Abstract read
In one paragraph

Article in Accounts of chemical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
11.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

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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

35 citing papers in PubMed, 260 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Hybrids of [FeFe]- and [NiFe]-HOrganometallics · 2023
    Article
  5. Enzymatic and Bioinspired Systems for Hydrogen Production.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Increasing the OACS catalysis · 2023
    Article
  8. Surprising Condensation Reactions of the Azadithiolate Cofactor.Angewandte Chemie (International ed. in English) · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Hydrogenase Mimics in MAngewandte Chemie (International ed. in English) · 2020
    Article
  13. The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Proton-Coupled Electron Transfer from Tyrosine in the Interior of aJournal of the American Chemical Society · 2020
    Article
  15. Article
  16. The final steps of [FeFe]-hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. MetalChemical science · 2019
    Article
  18. Redox and "Antioxidant" Properties of FeInorganic chemistry · 2019
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Thomas B RauchfussSchool of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
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 GM61153NIGMS NIH HHS R01 GM061153
6 · The paper itself

Abstract

The [FeFe] hydrogenases (H2ases) catalyze the redox reaction that interconverts protons and H2. This area of biocatalysis has attracted attention because the metal-based chemistry is unusual, and the reactions have practical implications. The active site consists of a [4Fe-4S] cluster bridged to a [Fe2(μ-dithiolate)(CN)2(CO)3](z) center (z = 1- and 2-). The dithiolate cofactor is [HN(CH2S)2](2-), called the azadithiolate ([adt(H)](2-)). Although many derivatives of Fe2(SR)2(CO)6-xLx are electrocatalysts for the hydrogen evolution reaction (HER), most operate by slow nonbiomimetic pathways. Biomimetic hydrogenogenesis is thought to involve intermediates, wherein the hydride substrate is adjacent to the amine of the adt(H), being bonded to only one Fe center. Formation of terminal hydride complexes is favored when the diiron carbonyl models contain azadithiolate. Although unstable in the free state, the adt cofactor is stable once it is affixed to the Fe2 center. It can be prepared by alkylation of Fe2(SH)2(CO)6 with formaldehyde in the presence of ammonia (to give adt(H) derivatives) or amines (to give adt(R) derivatives). Weak acids protonate Fe2(adt(R))(CO)2(PR3)4 to give terminal hydrido (term-H) complexes. In contrast, protonation of the related 1,3-propanedithiolate (pdt(2-)) complexes Fe2(pdt)(CO)2(PR3)4 requires strong acids. The amine in the azadithiolate is a kinetically fast base, relaying protons to and from the iron, which is a kinetically slow base. The crystal structure of the doubly protonated model [(term-H)Fe2(Hadt(H))(CO)2(dppv)2](2+) confirms the presence of both ammonium and terminal hydrido centers, which interact through a dihydrogen bond (dppv = cis-C2H2(PPh2)2). DFT calculations indicate that this H---H interaction is sensitive to the counterions and is strengthened upon reduction of the diiron center. For the monoprotonated models, the hydride [(term-H)Fe2(adt(H))(CO)2(dppv)2](+) exists in equilibrium with the ammonium tautomer [Fe2(Hadt(H))(CO)2(dppv)2](+). Both [(term-H)Fe2(Hadt(H))(CO)2(dppv)2](2+) and [(term-H)Fe2(adt(H))(CO)2(dppv)2](+) are highly active electrocatalysts for HER. Catalysis is initiated by reduction of the diferrous center, which induces coupling of the protic ammonium center and the hydride ligand. In contrast, the propanedithiolate [(term-H)Fe2(pdt)(CO)2(dppv)2](+) is a poor electrocatalyst for HER. Oxidation of H2 has been demonstrated, starting with models for the oxidized state ("Hox"), for example, [Fe2(adt(H))(CO)3(dppv)(PMe3)](+). Featuring a distorted Fe(II)Fe(I) center, this Hox model reacts slowly with high pressures of H2 to give [(μ-H)Fe2(adt(H))(CO)3(dppv)(PMe3)](+). Highlighting the role of the proton relay, the propanedithiolate [Fe2(pdt)(CO)3(dppv)(PMe3)](+) is unreactive toward H2. The Hox-model + H2 reaction is accelerated in the presence of ferrocenium salts, which simulate the role of the attached [4Fe-4S] cluster. The redox-complemented complex [Fe2(adt(Bn))(CO)3(dppv)(FcP*)](n+) catalyzes both proton reduction and hydrogen oxidation (FcP* = (C5Me5)Fe(C5Me4CH2PEt2)).

Indexed as

Aza CompoundsCatalytic DomainHydrogenaseIron CompoundsIron-Sulfur ProteinsModels, MolecularMolecular ConformationStereoisomerismSulfhydryl CompoundsAza CompoundsHydrogenaseIron Compoundsiron hydrogenaseIron-Sulfur ProteinsSulfhydryl Compounds

Identifiers

PMID26079848
PMCPMC4797653
OpenAlexW2441626394

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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.