Enzymatic catalysis has fueled considerable interest from chemists due to its high efficiency
and selectivity. However, the structural complexity and vulnerability hamper the application …

The reaction takes place at a specialized metal center that dramatically increases the acidity
of H2 and leads to a heterolytic splitting of the molecule which is strongly accelerated by the …

Over the last 15 years, a plethora of research has provided major insights into the structure
and function of hydrogenase enzymes. This has led to the important development of …

Enzymes that depend on sophisticated electron transfer via ferredoxins (Fds) exhibit
outstanding catalytic capabilities, but despite decades of research, many of them are still not …

Irreversible inhibition by molecular oxygen (O 2) complicates the use of [FeFe]-
hydrogenases (HydA) for biotechnological hydrogen (H 2) production. Modification by O 2 of …

Relatively recent developments in metalloenzyme and organometallic chemistry have
targeted a growing link between these outwardly incongruous fields, giving birth to a merger …

The active site of the mononuclear Fe-hydrogenase (Hmd) is a unique non-heme Fe
enzyme involved in the catalytic activation of molecular H2. Apart from the nitrile hydratases …

Cleavage of the dihydrogen molecule to give a bound proton and hydride, its oxidation to
yield protons and electrons, and the converse of these two processes, are intrinsic to the use …

Wie viele Nachbarn? Die Synthese, Struktur und Reaktivität eines fünffach koordinierten
Modellkomplexes von [Fe]‐Hydrogenase werden beschrieben. Die Befunde legen nahe …

Abstract [Fe]‐hydrogenase, the third type of natural hydrogenase, is capable to
heterolytically activate hydrogen molecule and transfer the resulting hydride to an …