Ekaterina V. Pletneva
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.
- M.S. Higher Chemical College of the Russian Academy of Sciences
- Ph.D. Iowa State University
F. Zhong, S. L. Alden, R. P. Hughes, E. V. Pletneva “Comparing properties of common bioinorganic ligands with switchable variants of cytochrome c” Inorg. Chem. 2022, 61, 1207–1227.
M. E. Clay, J. H. Hammond, F. Zhong, X. Chen, C. H. Kowalski, A. J. Lee, M. S. Porter, C. S. Greene, E. V. Pletneva, D. A. Hogan “Pseudomonas aeruginosa lasR mutant fitness in microoxia is supported by an Anr-regulated oxygen-binding hemerythrin” Proc. Natl. Acad. Sci. U. S. A. 2020, 117, 3167-3173.
J. M. Carpenter, F. Zhong, M. J. Ragusa, R. O. Louro, D. A. Hogan, E. V. Pletneva “Structure and redox properties of the diheme electron carrier cytochrome c4 from Pseudomonas aeruginosa” J. Inorg. Biochem. 2020, 203, 110889.
Y. Deng, M. L. Weaver, K. R. Hoke, E. V. Pletneva “A heme propionate staples the cytochrome c structure for methionine ligation to the heme iron” Inorg. Chem. 2019, 58, 14085-14106.