The H2-evolving potential of [FeFe] hydrogenases is severely limited by the oxygen
sensitivity of this class of enzymes. Recent experimental studies on hydrogenase from C …

FeFe hydrogenases catalyze H2 oxidation and production using an “H-cluster”, where two
Fe ions are bound by an aza-dithiolate (adt) ligand. Various hypotheses have been …

Nature is a valuable source of inspiration in the design of catalysts, and various approaches
are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce …

The [FeFe]-hydrogenase catalytic site H cluster is a complex iron sulfur cofactor that is
sensitive to oxygen (O2). The O2 sensitivity is a significant barrier for production of hydrogen …

FeFe hydrogenases catalyze H2 oxidation and formation at an inorganic active site (the “H-
cluster”), which consists of a [Fe2 (CO) 3 (CN) 2 (dithiomethylamine)] subcluster covalently …

[FeFe] hydrogenases interconvert H2 into protons and electrons reversibly and efficiently.
The active site H-cluster is composed of two sites: a unique [2Fe] subcluster ([2Fe] H) …

The [FeFe]-hydrogenases ([FeFe] H2ases) catalyze reversible H2 activation at the H-cluster,
which is composed of a [4Fe–4S] H subsite linked by a cysteine thiolate to a bridged …

While a general model of H2 activation has been proposed for [FeFe]-hydrogenases, the
structural and biophysical properties of the intermediates of the H-cluster catalytic site have …

The [FeFe]-hydrogenase (HydA1) from green algae is the minimal enzyme for efficient
biological hydrogen (H2) production. Its active-site six-iron center (H-cluster) consists of a …

[FeFe]-Hydrogenases contain a H2-converting cofactor (H-cluster) in which a canonical [4Fe–
4S] cluster is linked to a unique diiron site with three carbon monoxide (CO) and two cyanide …