Structural aspects of [NiFe]-hydrogenases

AbstractEnzymes that naturally contain an organometallic complex are highly rare. Hydrogenases commonly include iron carbonyl(s) at the active site and play central roles in the hydrogen metabolism of microorganisms. [NiFe]-hydrogenases that harbor an Ni-Fe(CN)2CO complex at the active site most widely exist among organisms, compared with the other two types, [FeFe]- and [Fe]-hydrogenases. Since the first crystal structure report in 1995, structural information of the Ni-Fe cluster with various redox/substrate-bound states has been obtained, although details of the reaction mechanisms are poorly understood. While the subunit composition, physiological function, and spectroscopic/biochemical properties of [NiFe]-hydrogenases are diverse, structural information of only a limited group of the enzymes is available so far. In this paper, structural aspects of [NiFe]-hydrogenases are reviewed and recent progresses in understanding the mechanism of an O2-tolerant property of limited members and active site assembling of [NiFe]-hydrogenases are described.