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 …

Virtually all organosulfur compounds react with Fe (0) carbonyls to give the title complexes.
These reactions are reviewed in light of major advances over the past few decades, spurred …

Hydrogenase proteins catalyze the reversible conversion of molecular hydrogen to protons
and electrons. The most abundant hydrogenases contain a [NiFe] active site; these proteins …

Recently, substantial efforts had been made in the field of synthetic iron compounds as
structural and functional models of the hydrogenase enzyme active site for the purpose of …

As the [2Fe] H subsite models of [FeFe]-hydrogenases, a series of PNP-chelated and-
bridged diiron dithiolate complexes 1a–f and 2a–f together with the three related …

An important clue to the mechanism for O2 tolerance of certain [NiFe]-hydrogenases is the
conserved presence of a modified environment around the iron–sulfur cluster that is …

As a further exploration of the asymmetrically substituted diiron models for the active site of
[FeFe]-hydrogenases, two new types of small bite-angle aminodiphosphine [(Ph2P) 2NR; …

“Hyd-1”, produced by Escherichia coli, exemplifies a special class of [NiFe]-hydrogenase
that can sustain high catalytic H2 oxidation activity in the presence of O2 an intruder that …

Abstract [FeFe]-hydrogenases efficiently catalyze the hydrogen evolution reactions (HERs)
at rates of up to 10 4 s− 1 with low overpotentials in aqueous media. Although the small …

Conventional oxidation catalysts frequently exhibit limited selectivity, restricting their use in
industrial syntheses. In particular, for the continuous synthesis of complex active …