Abstract
The structure around the metal site of mavicyanin, a protein molecule with a copper site, was investigated in solution by using time-differential perturbed angular correlation of 117In. The electric field gradient (EFG) of the metal site was deduced from the measurement. It demonstrated that the site in a mutant-type mavicyanin, Thr15Ala-Mav, gives an EFG different from that in the wild-type mavicyanin does. The pH dependence of the EFG was also observed for both proteins.
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Yokoyama, A., Hashimoto, T., Ihara, K. et al. Measurement of electric field gradient at 117In on the Cu-site in mavicyanin by perturbed angular correlation of γ-rays. Hyperfine Interact 181, 69–73 (2008). https://doi.org/10.1007/s10751-008-9691-z
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DOI: https://doi.org/10.1007/s10751-008-9691-z