Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer

Human carbonic anhydrase II (HCA II) uses a Zn-bound OH(−)/H(2)O mechanism to catalyze the reversible hydration of CO(2). This catalysis also involves a separate proton transfer step, mediated by an ordered solvent network coordinated by hydrophilic residues. One of these residues, Tyr7, was previou...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:Proc Natl Acad Sci U S A
Päätekijät: Michalczyk, Ryszard, Unkefer, Clifford J., Bacik, John-Paul, Schrader, Tobias E., Ostermann, Andreas, Kovalevsky, Andrey Y., McKenna, Robert, Fisher, Suzanne Zoë
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 2015
Aiheet:
Biological Sciences
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC4426434/
https://ncbi.nlm.nih.gov/pubmed/25902526
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1502255112
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