A third type of hydrogenase catalyzing H2 activation

The activation of molecular hydrogen is of interest both from a chemical and biological viewpoint. The covalent bond of H, is strong (436 kJ mol(-1)). Its cleavage is catalyzed by metals or metal complexes in chemical hydrogenation reactions and by metalloenzymes named hydrogenases in microorganisms. Until recently only two types of hydrogenases are known, the [FeFe]hydrogenases and [NiFe]-hydrogenases. Both types, which are phylogenetically unrelated, harbor in their active site a dinuclear metal center with intrinsic CO and cyanide ligands and contain iron-sulfur clusters for electron transport as revealed by their crystal structures. Fifteen years ago a third type of phylogenetically unrelated hydrogenase was discovered, which has a mononuclear iron active site and is devoid of iron-sulfur clusters. It was initially referred to as "metal free" hydrogenase, but was later renamed iron-sulfur cluster-free hydrogenase or [Fe]-hydrogenase. In this review, we introduce first the [FeFe]-hydrogenases and [NiFe]-hydrogenases, and then focus on the structure and function of the iron-sulfur cluster-free hydrogenase (Hmd) and show that this enzyme contains an iron-containing cofactor. The low-spin iron is complexed by two intrinsic CO, one sulfar- and one or two N/O ligands and has one open coordination site, which is proposed to be the location of H-2 binding. (c) 2007 The Japan Chemical Journal Forum and Wiley Periodicals, Inc.