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- W2137174865 abstract "Quinones and quinoproteins are essential redox components and enzymes in biological systems. Here, we report the de novo design, synthesis, and properties of model four-α-helix bundle quinoproteins. The proteins were designed and constructed from three different helices with 21 or 22 amino acid residues by chemoselective ligation to a cyclic decapeptide template. A free cysteine unit is placed at the hydrophobic core of the protein for binding of ubiquinone-0 and menaquinone-0 through a thioether bond. The quinoproteins with molecular weights of 11–12 kDa were characterized by electrospray ionization mass spectrometry, UV/Vis spectroscopy, size-exclusion chromatography, circular dichroism measurements, 1H NMR spectroscopy, cyclic voltammetry, and redox-induced FTIR difference spectroscopy. The midpoint redox potentials at pH 8 in aqueous solution Em,8 of thioether conjugates with N-acetyl cysteine methyl ester were 89 mV and −63 mV and with a synthetic protein 229 mV and 249 mV versus standard hydrogen electrode (SHE) for ubiquinone-0 and menaquinone-0, respectively. Detailed redox-induced FTIR difference spectroscopic studies of the model compounds and quinoproteins show the special resonance features for CO bands at 1656–1660 and 1655–1665 cm−1 due to the sulfur substitution to ubiquinone-0 and menaquinone-0, respectively. The construction of model quinoproteins represents a significant step toward more complex artificial redox systems." @default.
- W2137174865 created "2016-06-24" @default.
- W2137174865 creator A5000422071 @default.
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- W2137174865 creator A5005030141 @default.
- W2137174865 creator A5060411899 @default.
- W2137174865 date "2006-09-18" @default.
- W2137174865 modified "2023-10-18" @default.
- W2137174865 title "De Novo Design, Synthesis, and Characterization of Quinoproteins" @default.
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- W2137174865 doi "https://doi.org/10.1002/chem.200501212" @default.
- W2137174865 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16819733" @default.
- W2137174865 hasPublicationYear "2006" @default.
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