Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate
J. B. Holmes, V. Liu, B. G. Caulkins, E. Hilario, R. K. Ghosh, V. N. Drago, R. P. Young, J. Romero, A. D. Gill, P. M. Bogie, J. Paulino, X. Wang, G. Riviere, Y. K. Bosken, J. Struppe, , L. J. Mueller
This paper uses NMR-assisted crystallography to determine the protonation states and structure of the tryptophan synthase α-aminoacrylate intermediate, revealing insights into its reactivity and catalytic mechanism.
bioRxiv · May 12, 2021Biophysics