Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87544, United States.
Biochemistry. 2011 Nov 8;50(44):9421-3. doi: 10.1021/bi201487b. Epub 2011 Oct 12.
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.
在 pH 值为 7.8 时,野生型人碳酸酐酶 II 的中子结构已被确定到 2.0 Å 分辨率。详细分析并与之前在 pH 值为 10.0 时确定的结构进行比较,表明活性位点中关键催化残基的质子化以及氢键水网络的重排存在重要差异。首次直接观察到从 Zn 结合溶剂到质子穿梭残基 His64 的完整氢键网络。