Publications by Dafa Chen | EPFL Graph Search

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[Fe]-hydrogenase has a single iron-containing active site that features an acylmethylpyridinol ligand. This unique ligand environment had yet to be reproduced in synthetic models; however the synthesis and reactivity of a new class of small molecule mimics ...

The thiolate ligand in the five-coordinate model complex 1 of [Fe]-hydrogenase is preferentially and reversibly protonated, even in the presence of an acyl ligand. The results suggest that the Cys176 thiolate ligand in [Fe]-hydrogenase can serve as the int ...

[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 ...

[Fe]-Hydrogenase catalyses the reversible hydrogenation of a methenyltetrahydromethanopterin substrate, which is an intermediate step during the methanogenesis from CO2 and H-2. The active site contains an iron-guanylylpyridinol cofactor, in which Fe2+ is ...

Hydrogenases are biological catalysts for hydrogen evolution and activation. While many model complexes of hydrogenases can catalyze the hydrogen evolution reaction, few of them can react with hydrogen. Here we review the hydrogen-activating models of hydr ...

A series of Fe complexes were synthesized and characterized as small molecule mimics for the active site of [Fe]-hydrogenase (Hmd). The collection includes both structurally new compounds and analogues of previously reported models. These complexes contain ...

The decomposition reaction of a water-soluble complex (see scheme; 1) in H2O confirms the existence of a unique bidentate pyridinol cofactor in [Fe]-hydrogenase. This unique moiety is confirmed for the first time by the decomposition of a well-defined mode ...

The negative triangularity tokamak (NTT) is a unique reactor concept based on 'power-handling-first' philosophy with the heat exhaust problem as the leading concern. The present paper exposes a reactor concept using L-mode edge based on NTT configuration, ...

The synthesis, structure, and reactivity of small-molecule models of [Fe]-hydrogenase are described. These models feature the intriguing acylmethylpyridinyl ligands found exclusively in the enzyme. ...

The synthesis, structure, and reactivity of a five-coordinate model complex of [Fe]-hydrogenase are described. The work suggests that the iron center in [Fe]-hydrogenases could be five-coordinate in the resting state. ...

A [FeIIFeII] dithiolate complex containing acyl and carbonyl ligands was synthesized. The diiron complex reacted with phosphine, cyanide, isocyanide, and CO to give monomeric FeII complexes reproducing the first coordination sphere of the active site of [F ...

A mononuclear iron bis(carbonyl) pyridonate complex (1), which exhibits several common structural features with the active site of the iron−sulfur cluster-free [Fe]- hydrogenase, was synthesized and characterized. Spectroscopic data of 1 suggests a 2+ oxid ...

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Synthesis and Reactivity of Mononuclear Iron Models of [Fe]-Hydrogenase that Contain an Acylmethylpyridinol Ligand

Reversible protonation of a thiolate ligand in an [Fe]-hydrogenase model complex

[Fe]-hydrogenase and Models Containing An Iron-Acyl Ligation

Reconstitution of [Fe]-hydrogenase using model complexes

Hydrogen-activating models of hydrogenases

Synthesis and Characterization of a Series of Model Complexes of the Active Site of [Fe]-Hydrogenase (Hmd)

A Pyridinol Acyl Cofactor in the Active Site of [Fe]-hydrogenase Evidenced by the Reactivity of Model Complexes

L-mode-edge negative triangularity tokamak reactor

[Fe]-Hydrogenase Models Featuring Acylmethylpyridinyl Ligands

A Five-Coordinate Iron Center in the Active Site of [Fe]-Hydrogenase: Hints from a Model Study

Reversible Dimerization of Mononuclear Models of [Fe]-hydrogenase

Synthesis and Reactivity of Iron Acyl Complexes Modeling the Active Site of [Fe]-Hydrogenase

An Iron Carbonyl Pyridonate Complex Related to the Active Site of the [Fe]-Hydrogenase (Hmd)