Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis
-
- 花園, 祐矢
- Department of Chemistry, Graduate School of Science, Kyoto University; Institute for Quantum Life Science, National Institutes for Quantum Science and Technology; Present address: Medical Research Institute, Tokyo Medical and Dental University
-
- 平野, 優
- Institute for Quantum Life Science, National Institutes for Quantum Science and Technology; JST, PRESTO
-
- 竹田, 一旗
- Department of Chemistry, Graduate School of Science, Kyoto University
-
- 日下, 勝弘
- Frontier Research Center for Applied Atomic Sciences, Ibaraki University
-
- 玉田, 太郎
- Institute for Quantum Life Science, National Institutes for Quantum Science and Technology
-
- 三木, 邦夫
- Department of Chemistry, Graduate School of Science, Kyoto University
説明
The planarity of the peptide bond is important for the stability and structure formation of proteins. However, substantial distortion of peptide bonds has been reported in several high-resolution structures and computational analyses. To investigate the peptide bond planarity, including hydrogen atoms, we report a 1.2-Å resolution neutron structure of the oxidized form of high-potential iron-sulfur protein. This high-resolution neutron structure shows that the nucleus positions of the amide protons deviate from the peptide plane and shift toward the acceptors. The planarity of the H─N─C═O plane depends strongly on the pyramidalization of the nitrogen atom. Moreover, the orientation of the amide proton of Cys⁷⁵ is different in the reduced and oxidized states, possibly because of the electron storage capacity of the iron-sulfur cluster.
収録刊行物
-
- Science Advances
-
Science Advances 8 (20), 2022-05
American Association for the Advancement of Science (AAAS)
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1050010776427669120
-
- ISSN
- 23752548
-
- HANDLE
- 2433/274106
-
- PubMed
- 35594350
-
- 本文言語コード
- en
-
- 資料種別
- journal article
-
- データソース種別
-
- IRDB
- Crossref
- KAKEN
- OpenAIRE
