The effect of mutations in the vicinity of the putative electron transfer path on the metal center of the electron transfer protein plastocyanin (spinacea) is investigated by monitoring the nuclear quadrupole interaction of 111mCd in Cd-derivatives of the protein via time differential perturbed angular correlation. The spectra for the wild type protein and the mutants were rather similar. All spectra exhibit a peculiar line profile which points towards a small scale intramolecular flexibility of the metal center.
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Tröger et al. (1996) studied this question.