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- W2040277828 endingPage "66" @default.
- W2040277828 startingPage "51" @default.
- W2040277828 abstract "Tyrosine radicals play catalytic roles in essential metalloenzymes. Their properties—midpoint potential, stability…—or environment varies considerably from one enzyme to the other. To understand the origin of these properties, the redox tyrosines are studied by a number of spectroscopic techniques, including Fourier transform infrared (FTIR) and resonance Raman (RR) spectroscopy. An increasing number of vibrational data are reported for the (modified-) redox active tyrosines in ribonucleotide reductases, photosystem II, heme catalase and peroxidases, galactose and glyoxal oxidases, and cytochrome oxidase. The spectral markers for the tyrosinyl radicals have been recorded on models of (substituted) phenoxyl radicals, free or coordinated to metals. We review these vibrational data and present the correlations existing between the vibrational modes of the radicals and their properties and interactions formed with their environment: we present that the ν7a(C–O) mode of the radical, observed both by RR and FTIR spectroscopy at 1480–1515 cm−1, is a sensitive marker of the hydrogen bonding status of (substituted)-phenoxyl and Tyr, while the ν8a(C–C) mode may probe coordination of the Tyr to a metal. For photosystem II, the information obtained by light-induced FTIR difference spectroscopy for the two redox tyrosines TyrD and TyrZ and their hydrogen bonding partners is discussed in comparison with those obtained by other spectroscopic methods." @default.
- W2040277828 created "2016-06-24" @default.
- W2040277828 creator A5076517704 @default.
- W2040277828 creator A5089784441 @default.
- W2040277828 date "2005-02-01" @default.
- W2040277828 modified "2023-10-15" @default.
- W2040277828 title "Vibrational spectroscopy to study the properties of redox-active tyrosines in photosystem II and other proteins" @default.
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