Synthetic hydrogenases: Incorporation of an iron carbonyl thiolate into a designed peptide

Anne K. Jones; Bruce R. Lichtenstein; Arnab Dutta; Gwyneth Gordon; P. Leslie Dutton

doi:10.1021/ja075116a

Synthetic hydrogenases: Incorporation of an iron carbonyl thiolate into a designed peptide

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

Arizona State University

Research output: Contribution to journal › Article

73 Citations (Scopus)

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.

Original language	English
Pages (from-to)	14844-14845
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	48
DOIs	https://doi.org/10.1021/ja075116a
Publication status	Published - Dec 5 2007

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ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

Cite this

Jones, A. K., Lichtenstein, B. R., Dutta, A., Gordon, G., & Dutton, P. L. (2007). Synthetic hydrogenases: Incorporation of an iron carbonyl thiolate into a designed peptide. Journal of the American Chemical Society, 129(48), 14844-14845. https://doi.org/10.1021/ja075116a

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Access to Document

10.1021/ja075116a