DC Field | Value | Language |
---|---|---|
dc.contributor.author | Fukuda, Y | - |
dc.contributor.author | Tsea, KM | - |
dc.contributor.author | Nakane, T | - |
dc.contributor.author | Nakatsu, T | - |
dc.contributor.author | Suzuki, M | - |
dc.contributor.author | Sugahara, M | - |
dc.contributor.author | Inoue, S | - |
dc.contributor.author | Masuda, T | - |
dc.contributor.author | Yumoto, F | - |
dc.contributor.author | Matsugaki, N | - |
dc.contributor.author | Nango, E | - |
dc.contributor.author | Tono, K | - |
dc.contributor.author | Joti, Y | - |
dc.contributor.author | Kameshima, T | - |
dc.contributor.author | Song, CY | - |
dc.contributor.author | Hatsui, T | - |
dc.contributor.author | Yabashi, M | - |
dc.contributor.author | Nureki, O | - |
dc.contributor.author | Murphy, MEP | - |
dc.contributor.author | Inoue, T | - |
dc.contributor.author | Iwata, S | - |
dc.contributor.author | Mizohata, E | - |
dc.date.accessioned | 2016-08-26T07:32:39Z | - |
dc.date.available | 2016-08-26T07:32:39Z | - |
dc.date.created | 2016-05-12 | - |
dc.date.issued | 2016-03-15 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.other | 2016-OAK-0000035684 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/29943 | - |
dc.description.abstract | Proton-coupled electron transfer (PCET), a ubiquitous phenomenon in biological systems, plays an essential role in copper nitrite reductase (CuNiR), the key metalloenzyme in microbial denitrification of the global nitrogen cycle. Analyses of the nitrite reduction mechanism in CuNiR with conventional synchrotron radiation crystallography (SRX) have been faced with difficulties, because X-ray photoreduction changes the native structures of metal centers and the enzyme-substrate complex. Using serial femtosecond crystallography (SFX), we determined the intact structures of CuNiR in the resting state and the nitrite complex (NC) state at 2.03- and 1.60-angstrom resolution, respectively. Furthermore, the SRX NC structure representing a transient state in the catalytic cycle was determined at 1.30-angstrom resolution. Comparison between SRX and SFX structures revealed that photoreduction changes the coordination manner of the substrate and that catalytically important His255 can switch hydrogen bond partners between the backbone carbonyl oxygen of nearby Glu279 and the side-chain hydroxyl group of Thr280. These findings, which SRX has failed to uncover, propose a redox-coupled proton switch for PCET. This concept can explain how proton transfer to the substrate is involved in intramolecular electron transfer and why substrate binding accelerates PCET. Our study demonstrates the potential of SFX as a powerful tool to study redox processes in metalloenzymes. | - |
dc.description.statementofresponsibility | open | - |
dc.language | English | - |
dc.publisher | National Academy of Science | - |
dc.relation.isPartOf | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.subject | TYPE-2 COPPER SITE | - |
dc.subject | X-RAY-DIFFRACTION | - |
dc.subject | ALCALIGENES-FAECALIS | - |
dc.subject | ACTIVE-SITE | - |
dc.subject | ELECTRON-TRANSFER | - |
dc.subject | HIGH-RESOLUTION | - |
dc.subject | NITROGEN-CYCLE | - |
dc.subject | SPECTROSCOPIC CHARACTERIZATION | - |
dc.subject | RHODOBACTER-SPHAEROIDES | - |
dc.subject | CATALYTIC PATHWAY | - |
dc.title | Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography | - |
dc.type | Article | - |
dc.contributor.college | 물리학과 | - |
dc.identifier.doi | 10.1073/PNAS.1517770113 | - |
dc.author.google | Yohta Fukuda, Ka Man Tse, Takanori Nakane, Toru Nakatsu, Mamoru Suzuki, Michihiro Sugahara, Shigeyuki Inoue, Tetsuya Masuda, Fumiaki Yumoto, Naohiro Matsugaki, Eriko Nango, Kensuke Tono, Yasumasa Joti | - |
dc.relation.volume | 113 | - |
dc.relation.issue | 11 | - |
dc.relation.startpage | 2928 | - |
dc.relation.lastpage | 2933 | - |
dc.contributor.id | 10084037 | - |
dc.relation.journal | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Conference Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.113, no.11, pp.2928 - 2933 | - |
dc.identifier.wosid | 000372014200050 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 2933 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 2928 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 113 | - |
dc.contributor.affiliatedAuthor | Song, CY | - |
dc.identifier.scopusid | 2-s2.0-84962320904 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 35 | - |
dc.description.scptc | 32 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | TYPE-2 COPPER SITE | - |
dc.subject.keywordPlus | X-RAY-DIFFRACTION | - |
dc.subject.keywordPlus | ALCALIGENES-FAECALIS | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | ELECTRON-TRANSFER | - |
dc.subject.keywordPlus | HIGH-RESOLUTION | - |
dc.subject.keywordPlus | NITROGEN-CYCLE | - |
dc.subject.keywordPlus | SPECTROSCOPIC CHARACTERIZATION | - |
dc.subject.keywordPlus | RHODOBACTER-SPHAEROIDES | - |
dc.subject.keywordPlus | CATALYTIC PATHWAY | - |
dc.subject.keywordAuthor | copper | - |
dc.subject.keywordAuthor | bioinorganic chemistry | - |
dc.subject.keywordAuthor | free electron laser | - |
dc.subject.keywordAuthor | SAD phasing | - |
dc.subject.keywordAuthor | damage-free structure | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
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