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

Roy, Souvik, Nguyen, Thuy-Ai D., Gan, Lu and Jones, Anne K. (2015) Biomimetic peptide-based models of [FeFe]-hydrogenases: utilization of phosphine-containing peptides. Dalton Transactions, 44 (33). pp. 14865-14876. ISSN 1477-9226

Full content URL: https://doi.org/10.1039/C5DT01796C

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Item Type:Article
Item Status:Live Archive

Abstract

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.

Keywords:Peptides and proteins, Biomimetics, Hydrogenases
Subjects:C Biological Sciences > C720 Biological Chemistry
F Physical Sciences > F100 Chemistry
F Physical Sciences > F161 Organometallic Chemistry
Divisions:College of Science > School of Chemistry
ID Code:40678
Deposited On:17 Apr 2020 08:59

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