期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 31, 页码 9151-9154出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201705512
关键词
hydronium ions; low-barrier hydrogen bonds; neutron diffraction; proton transfer pathway
资金
- JST CREST [JPMJCR1656]
- JSPS KAKENHI [JP15H00864, JP16H06560, JP26105012, JP26711008]
- Japan Agency for Medical Research and Development (AMED)
- Materials Integration for engineering polymers of Cross-ministerial Strategic Innovation Promotion Program (SIP)
- Interdisciplinary Computational Science Program in CCS, University of Tsukuba
- Grants-in-Aid for Scientific Research [15K21719, 26105001, 26105012] Funding Source: KAKEN
Neutron diffraction analysis studies reported an isolated hydronium ion (H3O+) in the interior of d-xylose isomerase (XI) and phycocyanobilin-ferredoxin oxidoreductase (PcyA). H3O+ forms hydrogen bonds (H-bonds) with two histidine side-chains and a backbone carbonyl group in PcyA, whereas H3O+ forms H-bonds with three acidic residues in XI. Using a quantum mechanical/molecular mechanical (QM/ MM) approach, we analyzed stabilization of H3O+ by the protein environment. QM/MM calculations indicated that H3O+ was unstable in the PcyA crystal structure, releasing a proton to an H-bond partner His88, producing H2O and protonated His88. On the other hand, H3O+ was stable in the XI crystal structure. H-bond partners of isolated H3O+ would be practically limited to acidic residues such as aspartic and glutamic acids in the protein environment.
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