Biological conversion of methane to methanol through genetic reassembly of native catalytic domains
DC Field | Value | Language |
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dc.contributor.author | Kim, Hyun Jin | - |
dc.contributor.author | Huh, June | - |
dc.contributor.author | Kwon, Young Wan | - |
dc.contributor.author | Park, Donghyun | - |
dc.contributor.author | Yu, Yeonhwa | - |
dc.contributor.author | Jang, Young Eun | - |
dc.contributor.author | Lee, Bo-Ram | - |
dc.contributor.author | Jo, Eunji | - |
dc.contributor.author | Lee, Eun Jung | - |
dc.contributor.author | Heo, Yunseok | - |
dc.contributor.author | Lee, Weontae | - |
dc.contributor.author | Lee, Jeewon | - |
dc.date.accessioned | 2021-09-01T16:58:25Z | - |
dc.date.available | 2021-09-01T16:58:25Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2019-04 | - |
dc.identifier.issn | 2520-1158 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/66471 | - |
dc.description.abstract | Methane monooxygenase (MMO), which exists in particulate (pMMO) or soluble forms (sMMO) in methanotrophic bacteria, is an industrially promising enzyme that catalyses oxidation of low-reactive methane and other carbon feedstocks into methanol and their corresponding oxidation products. However, the simple, fast and high-yield production of functionally active MMO, which has so far been unsuccessful despite diverse approaches based on either native methanotroph culture or recombinant expression systems, remains a major challenge for its industrial applications. Here we developed pMMO-mimetic catalytic protein constructs by genetically encoding the beneficial reassembly of catalytic domains of pMMO on apoferritin as a biosynthetic scaffold. This approach resulted in high-yield synthesis of stable and soluble protein constructs in Escherichia coli, which successfully retain enzymatic activity for methanol production with a turnover number comparable to that of native pMMO. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | METHYLOCOCCUS-CAPSULATUS BATH | - |
dc.subject | MONOOXYGENASE PMMO | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | ENZYME IMMOBILIZATION | - |
dc.subject | HUMAN FERRITIN | - |
dc.subject | ACTIVE-SITE | - |
dc.subject | IN-VIVO | - |
dc.subject | OXIDATION | - |
dc.subject | PROTEIN | - |
dc.subject | COPPER | - |
dc.title | Biological conversion of methane to methanol through genetic reassembly of native catalytic domains | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Huh, June | - |
dc.contributor.affiliatedAuthor | Kwon, Young Wan | - |
dc.contributor.affiliatedAuthor | Lee, Jeewon | - |
dc.identifier.doi | 10.1038/s41929-019-0255-1 | - |
dc.identifier.scopusid | 2-s2.0-85063758112 | - |
dc.identifier.wosid | 000464248600014 | - |
dc.identifier.bibliographicCitation | NATURE CATALYSIS, v.2, no.4, pp.342 - 353 | - |
dc.relation.isPartOf | NATURE CATALYSIS | - |
dc.citation.title | NATURE CATALYSIS | - |
dc.citation.volume | 2 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 342 | - |
dc.citation.endPage | 353 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Physical | - |
dc.subject.keywordPlus | METHYLOCOCCUS-CAPSULATUS BATH | - |
dc.subject.keywordPlus | MONOOXYGENASE PMMO | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | ENZYME IMMOBILIZATION | - |
dc.subject.keywordPlus | HUMAN FERRITIN | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | IN-VIVO | - |
dc.subject.keywordPlus | OXIDATION | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | COPPER | - |
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