Synthetic hydrogenases

Incorporation of an iron carbonyl thiolate into a designed peptide

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

Research output: Contribution to journalArticle

67 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 languageEnglish
Pages (from-to)14844-14845
Number of pages2
JournalJournal of the American Chemical Society
Volume129
Issue number48
DOIs
Publication statusPublished - Dec 5 2007

Fingerprint

Hydrogenase
Peptides
Catalytic Domain
Iron
Organometallics
Hydrogen
Enzymes
Oxidation
Molecules
iron hydrogenase
reversible hydrogenase

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Synthetic hydrogenases : Incorporation of an iron carbonyl thiolate into a designed peptide. / Jones, Anne Katherine; Lichtenstein, Bruce R.; Dutta, Arnab; Gordon, Gwyneth; Dutton, P. Leslie.

In: Journal of the American Chemical Society, Vol. 129, No. 48, 05.12.2007, p. 14844-14845.

Research output: Contribution to journalArticle

Jones, Anne Katherine ; Lichtenstein, Bruce R. ; Dutta, Arnab ; Gordon, Gwyneth ; Dutton, P. Leslie. / Synthetic hydrogenases : Incorporation of an iron carbonyl thiolate into a designed peptide. In: Journal of the American Chemical Society. 2007 ; Vol. 129, No. 48. pp. 14844-14845.
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