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.
authors.affiliation: Department of Biochemistry and Biophysics, Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. jonesak@asu.edu
authors.forename: Anne K
authors.initials: AK
authors.lastname: Jones
authors.forename: Bruce R
authors.initials: BR
authors.lastname: Lichtenstein
authors.forename: Arnab
authors.initials: A
authors.lastname: Dutta
authors.forename: Gwyneth
authors.initials: G
authors.lastname: Gordon
authors.forename: P Leslie
authors.initials: PL
authors.lastname: Dutton
mesh_terms: D001665:Binding Sites; D002942:Circular Dichroism; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry*; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D013053:Spectrophotometry
chemical_list: D008024:Ligands; D008667:Metalloproteins; D010455:Peptides; D006864:Hydrogenase; D003545:Cysteine