Great progress has been achieved in the field of homogeneous transition metal-based catalysis, however, as a general rule these solution based catalysts are still easily outperformed, both in terms of rates and selectivity, by their analogous enzyme counterparts, including structural mimics of the active site. This observation suggests that the features of the enzyme beyond the active site, i.e. the outer-coordination sphere, are important for their exceptional function. Directly mimicking the outer-coordination sphere requires the incorporation of amino acids and peptides as ligands for homogeneous catalysts. This effort has been attempted for many homogeneous catalysts which span the manifold of catalytic reactions and often require careful thought regarding solvent type, pH and characterization to avoid unwanted side reactions or catalyst decomposition. This article reviews the current capability of synthesizing and characterizing this often difficult category of metal-based catalysts. This work was funded by the DOE Office of Science Early Career Research Program through the Office of Basic Energy Sciences. Pacific Northwest National Laboratory is operated by Battelle for the U.S. Department of Energy.
Revised: April 10, 2013 |
Published: October 9, 2012
Citation
Shaw W.J. 2012.The outer-coordination sphere: incorporating amino acids and peptides as ligands for homogeneous catalysts to mimic enzyme function.Catalysis Reviews: Science and Engineering 54, no. 4:489-550.PNNL-SA-84738.doi:10.1080/01614940.2012.679453