Capturing the Catalytic Proton of Dihydrofolate Reductase: Implications for General Acid–Base Catalysis

This publication has 70 references indexed in Scilit:

• Neutron protein crystallography: A complementary tool for locating hydrogens in proteins
  Archives of Biochemistry and Biophysics, 2016
• Long‐Range Electrostatics‐Induced Two‐Proton Transfer Captured by Neutron Crystallography in an Enzyme Catalytic Site
  Angewandte Chemie International Edition, 2016
• Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallography
  Proceedings of the National Academy of Sciences, 2015
• Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential
  IUCrJ, 2015
• Near‐Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes
  Angewandte Chemie International Edition, 2012
• Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness
  Acta Crystallographica Section D Structural Biology, 2012
• Identification of the Elusive Hydronium Ion Exchanging Roles with a Proton in an Enzyme at Lower pH Values
  Angewandte Chemie International Edition, 2011
• Loop and Subdomain Movements in the Mechanism of Escherichia coli Dihydrofolate Reductase: Crystallographic Evidence^,
  Biochemistry, 1997
• Isomorphous Crystal Structures of Escherichia coli Dihydrofolate Reductase Complexed with Folate, 5-Deazafolate, and 5,10-Dideazatetrahydrofolate: Mechanistic Implications
  Biochemistry, 1995
• Dihydrofolate reductase as a therapeutic target
  The FASEB Journal, 1990