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Fe-only hydrogenase is a metalloenzyme that is found in a variety of organisms such as acetogenic, photosynthetic, nitrogen-fixing, methanogenic and sulfate reducing bacteria (Adams, 1990; Vignais & Billoud, 2007). It plays an important role on energy cycling in the biological systems. Fe-only hydrogenase can either metabolize hydrogen molecules to produce reducing equivalents or store reducing power in the format of molecular hydrogen (Fontecilla-Camps et al., 2007). The most intriguing part of Fe-only hydrogenase is its high efficiency (6 × 103 s-1) in H2 production at a mild potential (-0.1 to -0.5 V vs NHC) (Holm et al., 1996). Understanding mechanism of enzymatic hydrogen production will facilitate design of better biomimetic models of Fe-only hydrogenase for substitutes to expensive platinum working electrodes used in industrial hydrogen production (Cammack et al., 2001; Vincent et al., 2007).

Design of Biomimetic Models Related to the Active Sites of Fe-Only Hydrogenase