Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate

Autor: Jacob B. Holmes, Viktoriia Liu, Bethany G. Caulkins, Eduardo Hilario, Rittik K. Ghosh, Victoria N. Drago, Robert P. Young, Jennifer A. Romero, Adam D. Gill, Paul M. Bogie, Joana Paulino, Xiaoling Wang, Gwladys Riviere, Yuliana K. Bosken, Jochem Struppe, Alia Hassan, Jevgeni Guidoulianov, Barbara Perrone, Frederic Mentink-Vigier, Chia-en A. Chang, Joanna R. Long, Richard J. Hooley, Timothy C. Mueser, Michael F. Dunn, Leonard J. Mueller

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 119, iss 2
Proceedings of the National Academy of Sciences of the United States of America

Significance The determination of active site protonation states is critical for a full mechanistic understanding of enzymatic transformations. However, hydrogen atom positions are challenging to extract using the standard tools of structural biology

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08d7608d5aac5e21b95efa8324291114
https://doi.org/10.1073/pnas.2109235119

Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional

Autor: Alexander, Klein, Petra, Rovó, Varun V, Sakhrani, Yangyang, Wang, Jacob B, Holmes, Viktoriia, Liu, Patricia, Skowronek, Laura, Kukuk, Suresh K, Vasa, Peter, Güntert, Leonard J, Mueller, Rasmus, Linser

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America

Significance The atomic-level understanding of protein function and enzyme catalysis requires site-specific information on chemical properties such as protonation and hybridization states and chemical exchange equilibria. This information is encoded

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d4096d656600363e2a135ebc0f48b89d
https://pubmed.ncbi.nlm.nih.gov/35058365

Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate

Autor: Rittik K. Ghosh, Viktoriia Liu, Chia-en A. Chang, Jevgeni Guidoulianov, Gwladys Riviere, Leonard J. Mueller, Frederic Mentink-Vigier, Adam D. Gill, Bethany G. Caulkins, Timothy C. Mueser, Robert P. Young, Barbara Perrone, Alia Hassan, Michael F. Dunn, Xiaoling Wang, Jennifer Romero, Jochem Struppe, Richard J. Hooley, Joanna R. Long, Eduardo Hilario, Victoria N. Drago, Jacob B. Holmes, Yuliana K. Bosken, Joana Paulino, Paul M. Bogie

NMR-assisted crystallography – the synergistic combination of solid-state NMR, X-ray crystallography, and first-principles computational chemistry – holds remarkable promise for mechanistic enzymology: by providing atomic-resolution characterizat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::55fe2cbdcc5bcfcb45a194207a8354da
https://doi.org/10.1101/2021.05.12.443852