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

Journal Article · Sat Jan 01 00:00:00 EST 2011 · Biochemistry (American Chemical Society)

DOI:https://doi.org/10.1021/bi201487b· OSTI ID:1050304

Fisher, Zoe ^[1]; Langan, Paul ^[2]; Mustyakimov, Marat ^[1]; Kovalevsky, Andrey ^[1]

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1. Los Alamos National Laboratory (LANL)
2. ORNL

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

• Research Organization: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
• Sponsoring Organization: USDOE Laboratory Directed Research and Development (LDRD) Program
• DOE Contract Number: DE-AC05-00OR22725
• OSTI ID: 1050304
• Journal Information: Biochemistry (American Chemical Society), Vol. 50, Issue 44; ISSN 0006--2960
• Country of Publication: United States
• Language: English

Related Subjects

08 HYDROGEN
CARBONIC ANHYDRASE
HYDROGEN
NEUTRONS
PROTONS
RESIDUES
RESOLUTION
SOLVENTS
WATER