Miller, A. ., Yikilmaz, E. ., & Vathyam, S. . (2010). 15N-NMR characterization of His residues in and around the active site of FeSOD. Biochimica Et Biophysica Acta, 1804(2), 275-84. https://doi.org/10.1016/j.bbapap.2009.11.009

Yikilmaz, E. ., Porta, J. ., Grove, L. ., Vahedi-Faridi, A. ., Bronshteyn, Y. ., Brunold, T. ., … Miller, A. . (2007). How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts?. Journal of the American Chemical Society, 129(32), 9927-40. https://doi.org/10.1021/ja069224t (Original work published 2007)

Yikilmaz, E. ., Rodgers, D. ., & Miller, A. . (2006). The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase. Biochemistry, 45(4), 1151-61. https://doi.org/10.1021/bi051495d (Original work published 2006)

Maliekal, J. ., Karapetian, A. ., Vance, C. ., Yikilmaz, E. ., Wu, Q. ., Jackson, T. ., … Miller, A. . (2002). Comparison and contrasts between the active site PKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase. Journal of the American Chemical Society, 124(50), 15064-75. https://doi.org/10.1021/ja027319z (Original work published 2002)

Yikilmaz, E. ., Xie, J. ., Brunold, T. ., & Miller, A. . (2002). Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase. Journal of the American Chemical Society, 124(14), 3482-3. https://doi.org/10.1021/ja011220v (Original work published 2002)

Schwartz, A. ., Yikilmaz, E. ., Vance, C. ., Vathyam, S. ., Koder, R. ., & Miller, A. . (2000). Mutational and spectroscopic studies of the significance of the active site glutamine to metal ion specificity in superoxide dismutase. Journal of Inorganic Biochemistry, 80(3-4), 247-56. https://doi.org/10.1016/s0162-0134(00)00086-6 (Original work published 2000)