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 journalArticle

17 Citations (Scopus)

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)Fe<inf>2</inf>(CO)<inf>6</inf> or (μ-bdt)Fe<inf>2</inf>(CO)<inf>6</inf> (pdt = propane-1,3-dithiolate, bdt = benzene-1,2-dithiolate). Formation of the complexes was confirmed by UV/Vis, FTIR and <sup>31</sup>P 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
Volume44
Issue number33
DOIs
StatePublished - Jul 23 2015

Fingerprint

phosphine
Hydrogenase
Biomimetics
Peptides
Carbon Monoxide
Amino Acids
Electrocatalysis
Propane
Carboxylic Acids
Benzene
Anchors
Amides
Acetic Acid
Functional groups
Nuclear magnetic resonance spectroscopy
Lysine
Amines
Resins

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

Biomimetic peptide-based models of [FeFe]-hydrogenases : Utilization of phosphine-containing peptides. / Roy, Souvik; Nguyen, Thuy Ai D; Gan, Lu; Jones, Anne.

In: Dalton Transactions, Vol. 44, No. 33, 23.07.2015, p. 14865-14876.

Research output: Contribution to journalArticle

Roy, Souvik ; Nguyen, Thuy Ai D ; Gan, Lu ; Jones, Anne. / Biomimetic peptide-based models of [FeFe]-hydrogenases : Utilization of phosphine-containing peptides. In: Dalton Transactions. 2015 ; Vol. 44, No. 33. pp. 14865-14876.
@article{23756580ff73455f920202f07187d710,
title = "Biomimetic peptide-based models of [FeFe]-hydrogenases: Utilization of phosphine-containing peptides",
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.",
author = "Souvik Roy and Nguyen, {Thuy Ai D} and Lu Gan and Anne Jones",
year = "2015",
month = "7",
day = "23",
doi = "10.1039/c5dt01796c",
language = "English (US)",
volume = "44",
pages = "14865--14876",
journal = "Dalton Transactions",
issn = "1477-9226",
publisher = "Royal Society of Chemistry",
number = "33",

}

TY - JOUR

T1 - Biomimetic peptide-based models of [FeFe]-hydrogenases

T2 - Utilization of phosphine-containing peptides

AU - Roy, Souvik

AU - Nguyen, Thuy Ai D

AU - Gan, Lu

AU - Jones, Anne

PY - 2015/7/23

Y1 - 2015/7/23

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84938915785&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84938915785&partnerID=8YFLogxK

U2 - 10.1039/c5dt01796c

DO - 10.1039/c5dt01796c

M3 - Article

C2 - 26223293

AN - SCOPUS:84938915785

VL - 44

SP - 14865

EP - 14876

JO - Dalton Transactions

JF - Dalton Transactions

SN - 1477-9226

IS - 33

ER -