Biomimetic peptide-based models of [FeFe]-hydrogenases: Utilization of phosphine-containing peptides

Souvik Roy, Thuy Ai D Nguyen, Lu Gan, Anne Jones

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Two synthetic strategies for incorporating diiron analogues of [FeFe]-hydrogenases into short peptides via phosphine functional groups are described. First, utilizing the amine side chain of lysine as an anchor, phosphine carboxylic acids can be coupled via amide formation to resin-bound peptides. Second, artificial, phosphine-containing amino acids can be directly incorporated into peptides via solution phase peptide synthesis. The second approach is demonstrated using three amino acids each with a different phosphine substituent (diphenyl, diisopropyl, and diethyl phosphine). In total, five distinct monophosphine-substituted, diiron model complexes were prepared by reaction of the phosphine-peptides with diiron hexacarbonyl precursors, either (μ-pdt)Fe2(CO)6 or (μ-bdt)Fe2(CO)6 (pdt = propane-1,3-dithiolate, bdt = benzene-1,2-dithiolate). Formation of the complexes was confirmed by UV/Vis, FTIR and 31P NMR spectroscopy. Electrocatalysis by these complexes is reported in the presence of acetic acid in mixed aqueous-organic solutions. Addition of water results in enhancement of the catalytic rates.

Original languageEnglish (US)
Pages (from-to)14865-14876
Number of pages12
JournalDalton Transactions
Issue number33
StatePublished - Jul 23 2015

ASJC Scopus subject areas

  • Inorganic Chemistry


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