Neutron structure of human carbonic anhydrase II: a hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0

Biochemistry. 2011 Nov 8;50(44):9421-3. doi: 10.1021/bi201487b. Epub 2011 Oct 12.

Abstract

The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 Å resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Carbonic Anhydrase II / chemistry*
  • Carbonic Anhydrase II / metabolism
  • Catalytic Domain*
  • Crystallography, X-Ray
  • Humans
  • Hydrogen Bonding
  • Hydrogen-Ion Concentration
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Neutron Activation Analysis / methods
  • Protons
  • Solutions
  • Water / chemistry*
  • Water / metabolism

Substances

  • Isoenzymes
  • Protons
  • Solutions
  • Water
  • Carbonic Anhydrase II

Associated data

  • PDB/3TMJ