Full metadata record
DC Field | Value | Language |
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dc.citation.number | 1 | - |
dc.citation.startPage | 4557 | - |
dc.citation.title | NATURE COMMUNICATIONS | - |
dc.citation.volume | 11 | - |
dc.contributor.author | Kim, Jin Kyun | - |
dc.contributor.author | Lee, Cheol | - |
dc.contributor.author | Lim, Seon Woo | - |
dc.contributor.author | Andring, Jacob T. | - |
dc.contributor.author | Adhikari, Aniruddha | - |
dc.contributor.author | McKenna, Robert | - |
dc.contributor.author | Ghim, Cheol-Min | - |
dc.contributor.author | Kim, Chae Un | - |
dc.date.accessioned | 2023-12-21T17:07:25Z | - |
dc.date.available | 2023-12-21T17:07:25Z | - |
dc.date.created | 2020-09-23 | - |
dc.date.issued | 2020-09 | - |
dc.description.abstract | Why metalloenzymes often show dramatic changes in their catalytic activity when subjected to chemically similar but non-native metal substitutions is a long-standing puzzle. Here, we report on the catalytic roles of metal ions in a model metalloenzyme system, human carbonic anhydrase II (CA II). Through a comparative study on the intermediate states of the zinc-bound native CA II and non-native metal-substituted CA IIs, we demonstrate that the characteristic metal ion coordination geometries (tetrahedral for Zn2+, tetrahedral to octahedral conversion for Co2+, octahedral for Ni2+, and trigonal bipyramidal for Cu2+) directly modulate the catalytic efficacy. In addition, we reveal that the metal ions have a long-range (~10 Å) electrostatic effect on restructuring water network in the active site. Our study provides evidence that the metal ions in metalloenzymes have a crucial impact on the catalytic mechanism beyond their primary chemical properties. © 2020, The Author(s). | - |
dc.identifier.bibliographicCitation | NATURE COMMUNICATIONS, v.11, no.1, pp.4557 | - |
dc.identifier.doi | 10.1038/s41467-020-18425-5 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.scopusid | 2-s2.0-85090797188 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/48187 | - |
dc.identifier.url | https://www.nature.com/articles/s41467-020-18425-5 | - |
dc.identifier.wosid | 000607111200018 | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Elucidating the role of metal ions in carbonic anhydrase catalysis | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Science & Technology - Other Topics | - |
dc.relation.journalResearchArea | Multidisciplinary Sciences | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | HYDROGEN-BOND NETWORK | - |
dc.subject.keywordPlus | PROTEIN CRYSTALS | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | PROTON-TRANSFER | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ZINC | - |
dc.subject.keywordPlus | CO2 | - |
dc.subject.keywordPlus | MODEL | - |
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