抄録
Hydrogen is known as an ultimate clean energy source and is thus discussed as a future sustainable energy carrier. Hydrogenases catalyze the reversible oxidation of the molecular hydrogen. We report the crystal structure analysis of [NiFe] hydrogenase from sulfate reducer at subatomic resolution. The structure reveals that the hydride bridge between nickel and iron at the active site and the possible proton bound site at the cysteine residue, resulting from the initial heterolytic splitting of dihydrogen by the enzyme. This finally clarifies the initial step in the mechanism of hydrogen conversion.