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

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

Research output: Contribution to journal › Article › peer-review

100 Scopus citations

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 (US)
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
State	Published - Dec 5 2007

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja075116a

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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.",

author = "Anne Jones and Lichtenstein, {Bruce R.} and Arnab Dutta and Gwyneth Gordon and Dutton, {P. Leslie}",

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AU - Lichtenstein, Bruce R.

AU - Dutta, Arnab

AU - Gordon, Gwyneth

AU - Dutton, P. Leslie

PY - 2007/12/5

Y1 - 2007/12/5

N2 - [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.

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

Abstract

ASJC Scopus subject areas

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