Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO2 Capture by a Surface-Exposed [Fe4S4] Cluster
DC Field | Value | Language |
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dc.contributor.author | Rettberg, Lee A. | - |
dc.contributor.author | Kang, Wonchull | - |
dc.contributor.author | Stiebritz, Martin T. | - |
dc.contributor.author | Hiller, Caleb J. | - |
dc.contributor.author | Lee, Chi Chung | - |
dc.contributor.author | Liedtke, Jasper | - |
dc.contributor.author | Ribbe, Markus W. | - |
dc.contributor.author | Hu, Yilin | - |
dc.date.accessioned | 2021-05-13T02:40:18Z | - |
dc.date.available | 2021-05-13T02:40:18Z | - |
dc.date.created | 2021-05-13 | - |
dc.date.issued | 2019-07 | - |
dc.identifier.issn | 2150-7511 | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/40944 | - |
dc.description.abstract | Nitrogenase iron (Fe) proteins reduce CO2 to CO and/or hydrocarbons under ambient conditions. Here, we report a 2.4-angstrom crystal structure of the Fe protein from Methanosarcina acetivorans (MaNifH), which is generated in the presence of a reductant, dithionite, and an alternative CO2 source, bicarbonate. Structural analysis of this methanogen Fe protein species suggests that CO2 is possibly captured in an unactivated, linear conformation near the [Fe4S4] cluster of MaNifH by a conserved arginine (Arg) pair in a concerted and, possibly, asymmetric manner. Density functional theory calculations and mutational analyses provide further support for the capture of CO2 on MaNifH while suggesting a possible role of Arg in the initial coordination of CO2 via hydrogen bonding and electrostatic interactions. These results provide a useful framework for further mechanistic investigations of CO2 activation by a surface-exposed [Fe4S4] cluster, which may facilitate future development of FeS catalysts for ambient conversion of CO2 into valuable chemical commodities. IMPORTANCE This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO2 capture by a surface-exposed [Fe4S4] cluster point to the possibility of developing novel strategies for CO2 sequestration while providing the initial insights into the unique mechanism of FeS-based CO2 activation. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | American Society for Microbiology | - |
dc.relation.isPartOf | mBio | - |
dc.title | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO2 Capture by a Surface-Exposed [Fe4S4] Cluster | - |
dc.type | Article | - |
dc.identifier.doi | 10.1128/mBio.01497-19 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | mBio, v.10, no.4 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000481617000080 | - |
dc.citation.number | 4 | - |
dc.citation.title | mBio | - |
dc.citation.volume | 10 | - |
dc.contributor.affiliatedAuthor | Kang, Wonchull | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.subject.keywordAuthor | CO2 capture | - |
dc.subject.keywordAuthor | FeS cluster | - |
dc.subject.keywordAuthor | iron protein | - |
dc.subject.keywordAuthor | methanogen | - |
dc.subject.keywordAuthor | nitrogenase | - |
dc.subject.keywordPlus | ZETA VALENCE QUALITY | - |
dc.subject.keywordPlus | AZOTOBACTER-VINELANDII | - |
dc.subject.keywordPlus | FE-PROTEIN | - |
dc.subject.keywordPlus | BASIS-SETS | - |
dc.subject.keywordPlus | CARBON-DIOXIDE | - |
dc.subject.keywordPlus | CRYSTALLOGRAPHIC STRUCTURE | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | DEHYDROGENASE | - |
dc.subject.keywordPlus | MOSSBAUER | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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