Ha, Yang Hu, Heidi Higgins, Khadine Maroney, Michael Hedman, Britt Hodgson, Keith Solomon, Edward The Electronic Structure of the Metal Active Site Determines the Geometric Structure and Function of the Metalloregulator NikR NikR is a nickel-responsive metalloregulator protein that controls the level of Ni<sup>2+</sup> ions in living cells. Previous studies have shown that NikR can bind a series of first-row transition metal ions but binds to DNA with high affinity only as a Ni<sup>2+</sup> complex. To understand this metal selectivity, S K-edge X-ray absorption spectroscopy of NikR bound to different metal ions was used to evaluate the different electronic structures. The experimental results are coupled with density functional theory calculations on relevant models. This study shows that both the <i>Z</i><sub>eff</sub> of the metal ion and the donor nature of the ligands determine the electronic structure of the metal site. This impacts the geometric structure of the metal site and thus the conformation of the protein. This contribution of electronic structure to geometric structure can be extended to other metal selective metalloregulators. S K-edge X-ray absorption spectroscopy;DNA;Metalloregulator NikR NikR;first-row transition metal ions;metal site;nickel-responsive metalloregulator protein 2019-08-14
    https://acs.figshare.com/articles/journal_contribution/The_Electronic_Structure_of_the_Metal_Active_Site_Determines_the_Geometric_Structure_and_Function_of_the_Metalloregulator_NikR/9616412
10.1021/acs.biochem.9b00542.s001