Ekaterina V. Pletneva

Academic Appointments

Professor of Chemistry

Molecular switching mediated by metal ions is an important process in the folding and function of metalloproteins, biological cell signaling, electron transfer and catalysis. When transition metal ions are involved, protein conformational switching affects the metal site's redox activity and conversely redox reactions themselves can act as triggers of protein rearrangements, enabling redox sensing. Despite the prominent role of redox-linked conformational changes in biology, the mechanisms of these transformations are poorly understood. Elucidating the principles that govern these phenomena could provide valuable insights for the design of novel conformational drugs targeting protein redox activity as well as switchable components for molecular electronics and artificial photosynthesis.

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Contact

114 Burke
HB 6128

Education

  • M.S. Higher Chemical College of the Russian Academy of Sciences
  • Ph.D. Iowa State University

Selected Publications

  • J. F. Amacher, F. Zhong, G. P. Lisi, M. Q., Zhu, S. L. Alden, K. R. Hoke, D. R. Madden,  E. V. Pletneva “A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch” J. Am. Chem. Soc. 2015, 137, 8435–8449.

  • C. W. T. Leung, Y. Hong, J. Hanske, E. Zhao, S. Chen, E. V. Pletneva, B. Z. Tang "A superior fluorescent probe for detection of cardiolipin" Anal. Chem. 2014, 86, 1263-8.

  • J. Gu, S. Yang, A. J. Rajic, I. V. Kurnikov, T. R. Prytkova, E. V. Pletneva "Control of cytochrome c redox reactivity through intraprotein hydrogen-bonding network" Chem. Commun. 2014, 50, 5355-5357.

  • F. Zhong, G. P. Lisi, D. P. Collins, J. H. Dawson, E. V. Pletneva "Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins" Proc. Natl. Acad. Sci. U. S. A. 2014, 111, E306-15.

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Works In Progress

“Unraveling Folding Dynamics of Heme Proteins with Fluorescence Energy Transfer Kinetics;” “Comparative Analysis of the Effects of Different Osmolytes on Folding of Drk SH3 Domain”