Abstract
The stable tyrosine radical of ribonucleotide reductase (RNR) from Escherichia coli, Tyr 122 of the B2 subunit, exhibits single-exponential spin-lattice relaxation lunetics for T≤16 K and nonexponential spin-lattice relaxation kinetics at higher temperatures. Saturation-recovery transients of the tyrosine radical are analyzed using a model developed to treat the interaction of two paramagnets in a rigid lattice at a fixed distance apart but with a randon orientation in the static magnetic field
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