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 |
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Pages (from-to) | 14844-14845 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 129 |
Issue number | 48 |
DOIs | |
Publication status | Published - Dec 5 2007 |
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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 journal › Article
}
TY - JOUR
T1 - Synthetic hydrogenases
T2 - Incorporation of an iron carbonyl thiolate into a designed peptide
AU - Jones, Anne Katherine
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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UR - http://www.scopus.com/inward/citedby.url?scp=36849041652&partnerID=8YFLogxK
U2 - 10.1021/ja075116a
DO - 10.1021/ja075116a
M3 - Article
C2 - 17997557
AN - SCOPUS:36849041652
VL - 129
SP - 14844
EP - 14845
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 48
ER -