Abstract 'Oxygen-tolerant'[NiFe]-hydrogenases can catalyze H 2 oxidation under aerobic
conditions, avoiding oxygenation and destruction of the active site. In one mechanism …

“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 …

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

The crystal structure of the membrane-bound O2-tolerant [NiFe]-hydrogenase 1 from
Escherichia coli (Ec Hyd-1) has been solved in three different states: as-isolated, H2 …

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 …

The active site of Hyd-1, an oxygen-tolerant membrane-bound [NiFe]-hydrogenase from
Escherichia coli, contains four highly conserved residues that form a “canopy” above the …

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

An oxygen-tolerant respiratory [NiFe]-hydrogenase is proven to be a four-electron
hydrogen/oxygen oxidoreductase, catalyzing the reaction 2 H2+ O2= 2 H2O, equivalent to …

[NiFe] hydrogenases are enzymes that catalyze the splitting of molecular hydrogen
according to the reaction H2→ 2H++ 2e–. Most of these enzymes are inhibited even by low …

[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 …