Onoda Akira, Hayashi Takashi
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 5650871, Japan.
Curr Opin Chem Biol. 2015 Apr;25:133-40. doi: 10.1016/j.cbpa.2014.12.041. Epub 2015 Jan 21.
Hydrogenase catalyses reversible transformation of H2 to H(+) using an active site which includes an iron or nickel atom. Synthetic model complexes and molecular catalysts inspired by nature have unveiled the structural and functional basis of the active site with remarkable accuracy and this has led to the discovery of active synthetic catalysts. To further improve the activity of such molecular catalysts, both the first and outer coordination spheres should be well-organized and harmonized for an efficient shuttling of H(+), electrons, and H2. This article reviews recent advances in the design and catalytic properties of artificial enzymes that mimic the hydrogenase active site and the outer coordination sphere in combination with a peptide or protein scaffold.
