Synthetic hydrogenases: incorporation of an iron carbonyl thiolate into a designed peptide.
[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.
Jones
Anne K
AK
Department of Biochemistry and Biophysics, Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. jonesak@asu.edu
Lichtenstein
Bruce R
BR
Dutta
Arnab
A
Gordon
Gwyneth
G
Dutton
P Leslie
PL
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
D008024:Ligands; D008667:Metalloproteins; D010455:Peptides; D006864:Hydrogenase; D003545:Cysteine