Synthesis of Tungsten and Molybdenum Carbon DioxideComplexes

Synthesis of Tungsten and Molybdenum Carbon Dioxide
Complexes:

Organometallics

DOI: 10.1021/om4002022

N–N Bond Cleavage of Hydrazines with a Multiproton-ResponsivePincer-Type Iron Complex

N–N Bond Cleavage of Hydrazines with a Multiproton-Responsive
Pincer-Type Iron Complex:

Journal of the American Chemical Society

DOI: 10.1021/ja3122944

EPR and FTIR Analysis of the Mechanism of H2 Activation by [FeFe]-Hydrogenase HydA1 from Chlamydomonasreinhardtii

EPR and FTIR Analysis of the Mechanism of H2 Activation by [FeFe]-Hydrogenase HydA1 from Chlamydomonas
reinhardtii:

Journal of the American Chemical Society

DOI: 10.1021/ja4000257

Catalytic hydrogen production by a Ni-Ru mimic of NiFe hydrogenases involves a proton-coupled electron transfer step

Catalytic hydrogen production by a Ni-Ru mimic of NiFe hydrogenases involves a proton-coupled electron transfer step:

Chem. Commun., 2013, Advance Article
DOI: 10.1039/C3CC40987B, Communication

Sigolene Canaguier, Vincent Fourmond, Carlo U. Perotto, Jennifer Fize, Jacques Pecaut, Marc Fontecave, Martin J. Field, Vincent Artero
Hydrogen evolution from weak acids catalyzed by a structural mimic of the active site of NiFe hydrogenases [Ni(xbsms)Ru(C₆Me₆)Cl]⁺ proceeds through proton-coupled electron transfer steps.
To cite this article before page numbers are assigned, use the DOI form of citation above.
The content of this RSS Feed (c) The Royal Society of Chemistry

Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases

Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases:

Insights in active sites: Hydrogen-conversion by hydrogenase is mediated by a sophisticated, metal-containing catalytic center. Resonance Raman spectroscopy is used for the first time in the characterization of the active site of these biocatalysts. An integrated spectroscopic and computational approach gives insights into structural and photochemical properties of the active site of an oxygen-tolerant [NiFe] hydrogenase.

[Fe]-Hydrogenase and Models that Contain IronAcyl Ligation

[Fe]-Hydrogenase and Models that Contain Iron<img src="http://onlinelibrarystatic.wiley.com/undisplayable_characters/00f8ff.gif" alt="[BOND]">Acyl Ligation:

Abstract

[Fe]-hydrogenase is a newly characterized type of hydrogenase. This enzyme heterolytically splits hydrogen in the presence of a natural substrate. The active site of the enzyme contains a mono-iron complex with intriguing ironacyl ligation. Several groups have recently developed ironacyl complexes as synthetic models of [Fe]-hydrogenase. This Focus Review summarizes the studies of this enzyme and its model compounds, with an emphasis on our own research in this area.

Plenty of [Fe]s in the fire: Recent studies on the structure and properties of [Fe]-hydrogenase have revealed the presence of a mono-iron-containing active site with ironacyl ligation. A number of synthetic complexes with this type of ligation have been prepared as models of this active site.

Exceptional Dendrimer-Based Mimics of Diiron Hydrogenase for the Photochemical Production of Hydrogen

Exceptional Dendrimer-Based Mimics of Diiron Hydrogenase for the Photochemical Production of Hydrogen:

A three-component homogeneous catalyst system has been prepared with an Ir^III complex as the photosensitizer, artificial hydrogenases bearing a diiron core and dendritic frameworks as the proton reduction catalyst, and triethylamine as the sacrificial electron donor. An initial turnover frequency of over 7240 h⁻¹ and a quantum yield of up to 28 % were determined for the photocatalytic evolution of hydrogen.

Nonprecious-Metal-Assisted Photochemical HydrogenProduction from ortho-Phenylenediamine

Nonprecious-Metal-Assisted Photochemical Hydrogen
Production from ortho-Phenylenediamine:

Journal of the American Chemical Society

DOI: 10.1021/ja4025116

Ferracyclic carbamoyl complexes related to the active site of [Fe]-hydrogenase

Ferracyclic carbamoyl complexes related to the active site of [Fe]-hydrogenase:

, 2013, Accepted Manuscript
DOI: 10.1039/C3DT50642H, Paper

Peter J Turrell, Amanda D Hill, Saad Khalil Ibrahim, Joseph A Wright, C J Pickett
The active site of the [Fe]-hydrogenase features an iron(II) centre bearing cis carbonyl groups and a chelating pyridine-acyl ligand. Reproducing these unusual features in synthetic models is an intriguing challenge,...
The content of this RSS Feed (c) The Royal Society of Chemistry

Reversible Dimerization of Mononuclear Models of [Fe]-Hydrogenase

Reversible Dimerization of Mononuclear Models of [Fe]-Hydrogenase:

Enzyme models on the catwalk! A series of new model complexes of the active site of [Fe]-hydrogenase have been synthesized and characterized. These complexes are monomeric in solution, but dimeric in the solid state.

Protonationof Ferrous Dinitrogen Complexes Containinga Diphosphine Ligand with a Pendent Amine

Protonation
of Ferrous Dinitrogen Complexes Containing
a Diphosphine Ligand with a Pendent Amine:

Inorganic Chemistry

DOI: 10.1021/ic4000704

I only post this (although it might already be on here) to see if anyone noticed that they used the same ReactIR 15 that we have - OU

cis-1,3,5-Triaminocyclohexane as a Facially Capping Ligand for Ruthenium(II)

cis-1,3,5-Triaminocyclohexane as a Facially Capping Ligand for Ruthenium(II):

Inorganic Chemistry

DOI: 10.1021/ic302819j