J. Am. Chem. Soc., 129 (48), 14844 -14845, 2007. 10.1021/ja075116a S0002-7863(07)05116-5
Web Release Date: November 13, 2007

Copyright © 2007 American Chemical Society

Synthetic Hydrogenases: Incorporation of an Iron Carbonyl Thiolate into a Designed Peptide

Anne K. Jones,* Bruce R. Lichtenstein, Arnab Dutta, Gwyneth Gordon, and P. Leslie Dutton

Department of Biochemistry and Biophysics, Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, and Department of Chemistry and Biochemistry and School of Earth and Space Exploration, Arizona State University, Tempe, Arizona 85287

jonesak@asu.edu

Received July 10, 2007

Abstract:

[FeFe] hydrogenases catalyze reversible hydrogen oxidation at an unusual organometallic active site. Neither enzymatic studies nor synthesis of small molecule models has managed to elucidate the mechanisms of these enzymes. In this paper, we demonstrate the incorporation of an iron carbonyl thiolate mimic of the hydrogenase active site into a de novo artificial peptide, creating the first peptide-based model system for hydrogenases.


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