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

78 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

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

Access to Document

10.1021/ja075116a

Fingerprint Dive into the research topics of 'Synthetic hydrogenases: Incorporation of an iron carbonyl thiolate into a designed peptide'. Together they form a unique fingerprint.

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

@article{6f8b4cb44fbd463bb965495fac26bae0,

title = "Synthetic hydrogenases: Incorporation of an iron carbonyl thiolate into a designed peptide",

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

year = "2007",

month = dec,

day = "5",

doi = "10.1021/ja075116a",

language = "English",

volume = "129",

pages = "14844--14845",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "48",

}

TY - JOUR

T1 - Synthetic hydrogenases

T2 - Incorporation of an iron carbonyl thiolate into a designed peptide

AU - Jones, Anne K.

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.

UR - http://www.scopus.com/inward/record.url?scp=36849041652&partnerID=8YFLogxK

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 -