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3-Aminotyrosine (NH 2 Y) has been a useful probe to study the role of redox active tyrosines in enzymes. This report describes properties of NH 2 Y of key importance for its application in mechanistic studies. By combining the tRNA/NH 2 Y-RS suppression technology with a model protein tailored for amino acid redox studies (α 3 X, X = NH 2 Y), the formal reduction potential of NH 2 Y 32 (O • /OH) ( E°' = 395 ± 7 mV at pH 7.08 ± 0.05) could be determined using protein film voltammetry. We find that the Δ E°' between NH 2 Y 32 (O • /OH) and Y 32 (O • /OH) when measured under reversible conditions is ∼300-400 mV larger than earlier estimates based on irreversible voltammograms obtained on aqueous NH 2 Y and Y. We have also generated D 6 -NH 2 Y 731 -α2 of ribonucleotide reductase (RNR), which when incubated with β2/CDP/ATP generates the D 6 -NH 2 Y 731  • -α2/β2 complex. By multifrequency electron paramagnetic resonance (35, 94, and 263 GHz) and 34 GHz 1 H ENDOR spectroscopies, we determined the hyperfine coupling (hfc) constants of the amino protons that establish RNH 2  • planarity and thus minimal perturbation of the reduction potential by the protein environment. The amount of Y in the isolated NH 2 Y-RNR incorporated by infidelity of the tRNA/NH 2 Y-RS pair was determined by a generally useful LC-MS method. This information is essential to the utility of this NH 2 Y probe to study any protein of interest and is employed to address our previously reported activity associated with NH 2 Y-substituted RNRs.

biochemistry

Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: <i>Escherichia coli</i> Ribonucleotide Reductase as a Paradigm

Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm