Normal modes of redox-active tyrosine: Conformation dependence and comparison to experiment

Article Abstract:

The Fourier transform infrared (FT-IR) results obtained from the characterizations of tyrosinate, tyrosyl radical and their isotopologues at 77 K are illustrated. The obtained results are compared to vibrational spectra associated with the oxidation of a redox active tyrosine in photosystem II (PS II), the photosynthetic water splitting enzyme.

Analysis, Usage, Oxidation-reduction reaction, Oxidation-reduction reactions, Fourier transform infrared spectroscopy, Photosynthesis

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Redox-active tyrosine residues in pentapeptides

Article Abstract:

The spectroscopic properties of tyrosyl radicals at 85 K is studied to develop the understanding of the effect of protein sequence on photophysical properties. The sequence of the pentapeptides is chosen to mimic peptide sequences found in redox-active tyrosine containing enzymes, ribonucleotide reductase and photosystem II.

Amino acid sequence, Amino acid sequencing

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ESEEM studies of peptide nitrogen hyperfine coupling in tyrosyl radicals and model peptides

Article Abstract:

A study report on [super 14]N- and [super 15]N-electron spin echo envelope modulation of model tyrosyl radical aimed at measuring weak hyperfine couplings to the amine nitrogen which reveal sequence- or conformation-induced changes in the ionic character of the NH bond in different tyrosine-containing peptides is presented.

Amines

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