Hydrogenases are essential for H2 cycling in microbial metabolism and serve as valuable
blueprints for H2-based biotechnological applications. However, most hydrogenases are …

Abstract [NiFe]‐hydrogenases catalyze the oxidation of H2 to protons and electrons. This
reversible reaction is based on a complex interplay of metal cofactors including the Ni–Fe …

Hydrogenases are abundant enzymes that catalyse the reversible interconversion of H2 into
protons and electrons at high rates. Those hydrogenases maintaining their activity in the …

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 …

[NiFe] hydrogenases catalyze the reversible splitting of H2 into protons and electrons at a
deeply buried active site. The catalytic center can be accessed by gas molecules through a …

Hydrogenases catalyze the reversible oxidation of H2 into protons and electrons and are
usually readily inactivated by O2. However, a subgroup of the [NiFe] hydrogenases …

Hydrogenases, abundant proteins in the microbial world, catalyze cleavage of H 2 into
protons and electrons or the evolution of H 2 by proton reduction. Hydrogen metabolism …

Hydrogenases catalyze the reversible conversion of molecular hydrogen to protons and
electrons via a heterolytic splitting mechanism. The active sites of [NiFe] hydrogenases …

“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 Membrane-bound respiratory [NiFe]-hydrogenase (MBH), a H2-uptake enzyme
found in the periplasmic space of bacteria, catalyses the oxidation of dihydrogen: H2→ …