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
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Carbonic Anhydrase II / chemistry*
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Carbonic Anhydrase II / metabolism
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Catalytic Domain*
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Crystallography, X-Ray
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Humans
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Hydrogen Bonding
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Hydrogen-Ion Concentration
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Isoenzymes / chemistry
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Isoenzymes / metabolism
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Neutron Activation Analysis / methods
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Protons
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Solutions
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Water / chemistry*
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Water / metabolism
Substances
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Isoenzymes
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Protons
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Solutions
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Water
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Carbonic Anhydrase II