PNNL

Abstract

The reversible reduction of protons to dihydrogen is deceptively the simplest of reactions but one which requires multi-step catalysis to proceed at practical rates. How the metal-sulfur of the hydrogenases catalyse this interconversion has been the subject has been the subject of intensive structural, spectroscopic and mechanistic studies of the enzymes, of synthetic assemblies and of in silico models. Beyond the intrinsic desire to understand how metallo-sulfur clusters in biology catalyses a range of difficult chemistry, including nitrogen fixation, research on hydrogenase chemistry is particularly driven by the view that understanding active-site structure and function will inform the design of new materials for hydrogen production or uptake, pertinent to energy transduction technology and a hydrogen economy. Herein we report the assembly of the first materials with di-iron sub-sites linked by a thiolate bridge to a {4Fe4S} – cluster, as found at the active site of the iron-only hydrogenase, the H-cluster.