Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein
DC Field | Value | Language |
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dc.contributor.author | Rettberg, Lee A. | - |
dc.contributor.author | Stiebritz, Martin T. | - |
dc.contributor.author | Kang, Wonchull | - |
dc.contributor.author | Lee, Chi Chung | - |
dc.contributor.author | Ribbe, Markus W. | - |
dc.contributor.author | Hu, Yilin | - |
dc.date.accessioned | 2021-05-13T02:40:17Z | - |
dc.date.available | 2021-05-13T02:40:17Z | - |
dc.date.created | 2021-05-13 | - |
dc.date.issued | 2019-10 | - |
dc.identifier.issn | 0947-6539 | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/40943 | - |
dc.description.abstract | The Fe protein of nitrogenase catalyzes the ambient reduction of CO2 when its cluster is present in the all-ferrous, [Fe4S4](0) oxidation state. Here, we report a combined structural and theoretical study that probes the unique reactivity of the all-ferrous Fe protein toward CO2. Structural comparisons of the Azotobacter vinelandii Fe protein in the [Fe4S4](0) and [Fe4S4](+) states point to a possible asymmetric functionality of a highly conserved Arg pair in CO2 binding and reduction. Density functional theory (DFT) calculations provide further support for the asymmetric coordination of O by the "proximal" Arg and binding of C to a unique Fe atom of the all-ferrous cluster, followed by donation of protons by the proximate guanidinium group of Arg that eventually results in the scission of a C-O bond. These results provide important mechanistic and structural insights into CO2 activation by a surface-exposed, scaffold-held [Fe4S4] cluster. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.relation.isPartOf | CHEMISTRY-A EUROPEAN JOURNAL | - |
dc.title | Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein | - |
dc.type | Article | - |
dc.identifier.doi | 10.1002/chem.201903387 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | CHEMISTRY-A EUROPEAN JOURNAL, v.25, no.57, pp.13078 - 13082 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000489795500003 | - |
dc.citation.endPage | 13082 | - |
dc.citation.number | 57 | - |
dc.citation.startPage | 13078 | - |
dc.citation.title | CHEMISTRY-A EUROPEAN JOURNAL | - |
dc.citation.volume | 25 | - |
dc.contributor.affiliatedAuthor | Kang, Wonchull | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.subject.keywordAuthor | all-ferrous | - |
dc.subject.keywordAuthor | C1 reduction | - |
dc.subject.keywordAuthor | carbon dioxide | - |
dc.subject.keywordAuthor | iron proteins | - |
dc.subject.keywordAuthor | nitrogenase | - |
dc.subject.keywordPlus | FERROUS FE4S4 CLUSTER | - |
dc.subject.keywordPlus | FE-PROTEIN | - |
dc.subject.keywordPlus | AZOTOBACTER-VINELANDII | - |
dc.subject.keywordPlus | 2-HYDROXYGLUTARYL-COA DEHYDRATASE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | DEHYDROGENASE | - |
dc.subject.keywordPlus | MOSSBAUER | - |
dc.subject.keywordPlus | COMPONENT | - |
dc.subject.keywordPlus | STATE | - |
dc.subject.keywordPlus | FORM | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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