Synthesis of the H-cluster framework of iron-only hydrogenase

@article{Tard2005SynthesisOT,
  title={Synthesis of the H-cluster framework of iron-only hydrogenase},
  author={C{\'e}dric Tard and Xiaoming Liu and Saad K. Ibrahim and Maurizio Bruschi and Luca De Gioia and S{\^i}an C. Davies and Xin Yang and Lai‐Sheng Wang and Gary Sawers and Christopher J. Pickett},
  journal={Nature},
  year={2005},
  volume={433},
  pages={610-613}
}
The metal-sulphur active sites of hydrogenases catalyse hydrogen evolution or uptake at rapid rates. Understanding the structure and function of these active sites—through mechanistic studies of hydrogenases, synthetic assemblies and in silico models—will help guide the design of new materials for hydrogen production or uptake. Here we report the assembly of the iron-sulphur framework of the active site of iron-only hydrogenase (the H-cluster), and show that it functions as an electrocatalyst… 

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References

SHOWING 1-10 OF 56 REFERENCES

Chemistry and the hydrogenases.

The reversible reduction protons to dihydrogen: 2H+ + 2e [symbol: see text] H2 is deceptively the simplest of reactions but one that requires multistep catalysis to proceed at practical rates. How

Electronic Structure of the H Cluster in [Fe]-Hydrogenases

[Fe]-Hydrogenase II isolated from C. pasteurianum contains 14 Fe which are distributed among the so-called H cluster (the catalytic center) and two [4Fe-4S] clusters. Insights gained from Mossbauer

The di-iron subsite of all-iron hydrogenase: mechanism of cyanation of a synthetic [2Fe3S]-carbonyl assembly.

Stopped-flow FTIR spectroscopy has enabled the quantitation of the dynamics of five well-defined steps that experimentally illustrate the role of bridging carbonyls in the assembly of the dicyanide species, how on-off sulfur ligation can have a dramatic effect on cyanation kinetics and how the [2Fe3S] core stabilises bridgingcarbonyl species.

All-iron hydrogenase: synthesis, structure and properties of {2Fe3S}-assemblies related to the di-iron sub-site of the H-clusterElectronic supplementary information (ESI) available: crystal and structure refinement data for complexes 4a, 4b and 5a. See http://www.rsc.org/suppdata/dt/b2/b209690k/

Tripodal dithiolate thioether ligands MeC(CH2SH)2CH2SR (R = Me or Ph) provide a route to {2Fe3S}-complexes and syntheses are described. X-Ray crystal structures for two {2Fe3S}-pentacarbonyl

First Generation Analogues of the Binuclear Site in the Fe-Only Hydrogenases: Fe2(μ-SR)2(CO)4(CN)22-

Having cyanide and CO coligands as well as metal-metal bonding, the hydrogenase active sites represent a link between the otherwise disparate realms of organometallic and biological Fe-S chemistry.

Density functional theory investigation of the active site of Fe-hydrogenases. systematic study of the effects of redox state and ligands hardness on structural and electronic properties of complexes related to the [2Fe](H) subcluster.

Results show that the structural and electronic properties of fully reduced Fe(i)Fe(I) complexes are strongly affected by the nature of the ligand L, and in particular, a progressive rotation of the Fe(d)(CO)(2)(CN) group, with a CO ligand moving from a terminal to a semibridged position, is observed going from the softest to the hardest ligand.

Modeling the active sites in metalloenzymes. 3. Density functional calculations on models for [Fe]-hydrogenase: structures and vibrational frequencies of the observed redox forms and the reaction mechanism at the Diiron Active Center.

  • Z. CaoM. Hall
  • Chemistry
    Journal of the American Chemical Society
  • 2001
The oxidation states and structures for the diiron active site are proposed, and a proposed reaction mechanism (catalytic cycle) based on the DFT calculations shows that heterolytic cleavage of H(2) can occur from (eta(2)-H(2)) Fe(II)-Fe(II) via a proton transfer to "spectator" ligands.

Carbon Monoxide and Cyanide Ligands in a Classical Organometallic Complex Model for Fe-Only Hydrogenase.

The Fe(I) organometallic complex provides a structural model for the cyano-carbonyl diiron site of Fe-only hydrogenase as characterized by X-ray crystallography.

A di-iron dithiolate possessing structural elements of the carbonyl/cyanide sub-site of the H-centre of Fe-only hydrogenase

The synthesis and characterisation of the first {2Fe2S}-cluster bearing both CO and CN ligands is described; the iron atoms are linked by the bridging 1,3-propanedithiolate unit that has been
...