Synthetic Hydrogenases: Incorporation of an Iron Carbonyl Thiolate into a Designed Peptide
- 13 November 2007
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 129 (48) , 14844-14845
- https://doi.org/10.1021/ja075116a
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.Keywords
This publication has 14 references indexed in Scilit:
- Characterization of a Diferrous Terminal Hydride Mechanistically Relevant to the Fe-Only HydrogenasesJournal of the American Chemical Society, 2005
- Synthesis of the H-cluster framework of iron-only hydrogenaseNature, 2005
- Structural and functional models related to the nickel hydrogenasesCoordination Chemistry Reviews, 2004
- Highly Active, Binary Catalyst Systems for the Alternating Copolymerization of CO2 and Epoxides under Mild ConditionsAngewandte Chemie International Edition in English, 2004
- Probing metallopeptide folding mechanisms using de novo design peptidesJournal of Inorganic Biochemistry, 2003
- Chemistry and the hydrogenasesChemical Society Reviews, 2003
- Hydrogen as a FuelPublished by Taylor & Francis ,2001
- Helix−Loop−Helix Peptides as Scaffolds for the Construction of Bridged Metal Assemblies in Proteins: The Spectroscopic A-Cluster Structure in Carbon Monoxide DehydrogenaseJournal of the American Chemical Society, 2001
- A 25,000-Year Tropical Climate History from Bolivian Ice CoresScience, 1998
- Toward the Synthesis of a Photosynthetic Reaction Center Maquette: A Cofacial Porphyrin Pair Assembled between Two Subunits of a Synthetic Four-Helix Bundle Multiheme ProteinJournal of the American Chemical Society, 1996