Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.
Identifieur interne : 000146 ( Main/Curation ); précédent : 000145; suivant : 000147Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.
Auteurs : Hirofumi Harada ; Akira Onoda ; Takayuki Uchihashi [Japon] ; Hiroki Watanabe [Japon] ; Naoki Sunagawa [Japon] ; Masahiro Samejima [Japon] ; Kiyohiko Igarashi [Japon, Finlande] ; Takashi HayashiSource :
- Chemical science [ 2041-6520 ] ; 2017.
Abstract
Cellobiose dehydrogenase (CDH) is a dual domain flavocytochrome, which consists of a dehydrogenase (DH) domain containing a flavin adenine dinucleotide and a cytochrome (CYT) domain containing b-type heme. To directly visualize the dynamic domain motion of class-I CDH from Phanerochaete chrysosporium (PcCDH) during catalysis using high-speed atomic force microscopy, the apo-form of PcCDH was anchored to a heme-immobilized flat gold surface that can specifically fix the orientation of the CYT domain. The two domains of CDH are found to be immobile in the absence of cellobiose, whereas the addition of cellobiose triggers an interdomain flip-flop motion involving domain-domain association and dissociation. Our results indicate that dynamic motion of a dual domain enzyme during catalysis induces efficient electron transfer to an external electron acceptor.
DOI: 10.1039/c7sc01672g
PubMed: 28989682
PubMed Central: PMC5627353
Links toward previous steps (curation, corpus...)
- to stream Main, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000146
Links to Exploration step
pubmed:28989682Curation
No country items
Hirofumi Harada<affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation>Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.</title><author><name sortKey="Harada, Hirofumi" sort="Harada, Hirofumi" uniqKey="Harada H" first="Hirofumi" last="Harada">Hirofumi Harada</name><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation></author><author><name sortKey="Onoda, Akira" sort="Onoda, Akira" uniqKey="Onoda A" first="Akira" last="Onoda">Akira Onoda</name><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation></author><author><name sortKey="Uchihashi, Takayuki" sort="Uchihashi, Takayuki" uniqKey="Uchihashi T" first="Takayuki" last="Uchihashi">Takayuki Uchihashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physics , Nagoya University , Furo-cho, Chikusa-ku , Nagoya , 464-8602 , Japan . Email: uchihast@d.phys.nagoya-u.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author><author><name sortKey="Watanabe, Hiroki" sort="Watanabe, Hiroki" uniqKey="Watanabe H" first="Hiroki" last="Watanabe">Hiroki Watanabe</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Natural Science and Technology , Kanazawa University , Kakuma , Kanazawa , 920-1192 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Natural Science and Technology , Kanazawa University , Kakuma , Kanazawa , 920-1192 </wicri:regionArea></affiliation></author><author><name sortKey="Sunagawa, Naoki" sort="Sunagawa, Naoki" uniqKey="Sunagawa N" first="Naoki" last="Sunagawa">Naoki Sunagawa</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author><author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation><affiliation wicri:level="1"><nlm:affiliation>VTT Technical Research Centre of Finland , P.O. Box 1000, Tietotie 2 , Espoo FI-02044 VTT , Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>VTT Technical Research Centre of Finland , P.O. Box 1000, Tietotie 2 , Espoo FI-02044 VTT </wicri:regionArea></affiliation></author><author><name sortKey="Hayashi, Takashi" sort="Hayashi, Takashi" uniqKey="Hayashi T" first="Takashi" last="Hayashi">Takashi Hayashi</name><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28989682</idno><idno type="pmid">28989682</idno><idno type="doi">10.1039/c7sc01672g</idno><idno type="pmc">PMC5627353</idno><idno type="wicri:Area/Main/Corpus">000146</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000146</idno><idno type="wicri:Area/Main/Curation">000146</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000146</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.</title><author><name sortKey="Harada, Hirofumi" sort="Harada, Hirofumi" uniqKey="Harada H" first="Hirofumi" last="Harada">Hirofumi Harada</name><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation></author><author><name sortKey="Onoda, Akira" sort="Onoda, Akira" uniqKey="Onoda A" first="Akira" last="Onoda">Akira Onoda</name><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation></author><author><name sortKey="Uchihashi, Takayuki" sort="Uchihashi, Takayuki" uniqKey="Uchihashi T" first="Takayuki" last="Uchihashi">Takayuki Uchihashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physics , Nagoya University , Furo-cho, Chikusa-ku , Nagoya , 464-8602 , Japan . Email: uchihast@d.phys.nagoya-u.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author><author><name sortKey="Watanabe, Hiroki" sort="Watanabe, Hiroki" uniqKey="Watanabe H" first="Hiroki" last="Watanabe">Hiroki Watanabe</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Natural Science and Technology , Kanazawa University , Kakuma , Kanazawa , 920-1192 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Natural Science and Technology , Kanazawa University , Kakuma , Kanazawa , 920-1192 </wicri:regionArea></affiliation></author><author><name sortKey="Sunagawa, Naoki" sort="Sunagawa, Naoki" uniqKey="Sunagawa N" first="Naoki" last="Sunagawa">Naoki Sunagawa</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation></author><author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country></affiliation><affiliation wicri:level="1"><nlm:affiliation>VTT Technical Research Centre of Finland , P.O. Box 1000, Tietotie 2 , Espoo FI-02044 VTT , Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>VTT Technical Research Centre of Finland , P.O. Box 1000, Tietotie 2 , Espoo FI-02044 VTT </wicri:regionArea></affiliation></author><author><name sortKey="Hayashi, Takashi" sort="Hayashi, Takashi" uniqKey="Hayashi T" first="Takashi" last="Hayashi">Takashi Hayashi</name><affiliation><nlm:affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</nlm:affiliation><wicri:noCountry code="subField">Japan </wicri:noCountry></affiliation></author></analytic><series><title level="j">Chemical science</title><idno type="ISSN">2041-6520</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellobiose dehydrogenase (CDH) is a dual domain flavocytochrome, which consists of a dehydrogenase (DH) domain containing a flavin adenine dinucleotide and a cytochrome (CYT) domain containing <i>b</i>-type heme. To directly visualize the dynamic domain motion of class-I CDH from <i>Phanerochaete chrysosporium</i> (<i>Pc</i>CDH) during catalysis using high-speed atomic force microscopy, the apo-form of <i>Pc</i>CDH was anchored to a heme-immobilized flat gold surface that can specifically fix the orientation of the CYT domain. The two domains of CDH are found to be immobile in the absence of cellobiose, whereas the addition of cellobiose triggers an interdomain flip-flop motion involving domain-domain association and dissociation. Our results indicate that dynamic motion of a dual domain enzyme during catalysis induces efficient electron transfer to an external electron acceptor.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">28989682</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">2041-6520</ISSN><JournalIssue CitedMedium="Print"><Volume>8</Volume><Issue>9</Issue><PubDate><Year>2017</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Chemical science</Title><ISOAbbreviation>Chem Sci</ISOAbbreviation></Journal><ArticleTitle>Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.</ArticleTitle><Pagination><MedlinePgn>6561-6565</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c7sc01672g</ELocationID><Abstract><AbstractText>Cellobiose dehydrogenase (CDH) is a dual domain flavocytochrome, which consists of a dehydrogenase (DH) domain containing a flavin adenine dinucleotide and a cytochrome (CYT) domain containing <i>b</i>-type heme. To directly visualize the dynamic domain motion of class-I CDH from <i>Phanerochaete chrysosporium</i> (<i>Pc</i>CDH) during catalysis using high-speed atomic force microscopy, the apo-form of <i>Pc</i>CDH was anchored to a heme-immobilized flat gold surface that can specifically fix the orientation of the CYT domain. The two domains of CDH are found to be immobile in the absence of cellobiose, whereas the addition of cellobiose triggers an interdomain flip-flop motion involving domain-domain association and dissociation. Our results indicate that dynamic motion of a dual domain enzyme during catalysis induces efficient electron transfer to an external electron acceptor.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Harada</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Onoda</LastName><ForeName>Akira</ForeName><Initials>A</Initials><Identifier Source="ORCID">0000-0002-5791-4386</Identifier><AffiliationInfo><Affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Uchihashi</LastName><ForeName>Takayuki</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Physics , Nagoya University , Furo-cho, Chikusa-ku , Nagoya , 464-8602 , Japan . Email: uchihast@d.phys.nagoya-u.ac.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Watanabe</LastName><ForeName>Hiroki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Faculty of Natural Science and Technology , Kanazawa University , Kakuma , Kanazawa , 920-1192 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sunagawa</LastName><ForeName>Naoki</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials><Identifier Source="ORCID">0000-0001-5152-7177</Identifier><AffiliationInfo><Affiliation>Department of Biomaterials Sciences , Graduate School of Agricultural and Life Sciences , The University of Tokyo , Bunkyo-ku , 113-8657 , Japan . Email: aquarius@mail.ecc.u-tokyo.ac.jp.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>VTT Technical Research Centre of Finland , P.O. Box 1000, Tietotie 2 , Espoo FI-02044 VTT , Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hayashi</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0002-2215-935X</Identifier><AffiliationInfo><Affiliation>Department of Applied Chemistry , Graduate School of Engineering , Osaka University , 2-1 Yamadaoka , Suita , Osaka 565-0871 , Japan . Email: onoda@chem.eng.osaka-u.ac.jp ; Email: thayashi@chem.eng.osaka-u.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>08</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Chem Sci</MedlineTA><NlmUniqueID>101545951</NlmUniqueID><ISSNLinking>2041-6520</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>04</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>07</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>10</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28989682</ArticleId><ArticleId IdType="doi">10.1039/c7sc01672g</ArticleId><ArticleId IdType="pii">c7sc01672g</ArticleId><ArticleId IdType="pmc">PMC5627353</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Chemistry. 2000 Feb 18;6(4):592-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10807170</ArticleId></ArticleIdList></Reference><Reference><Citation>J Proteome Res. 2011 Sep 2;10(9):4177-85</Citation><ArticleIdList><ArticleId IdType="pubmed">21744778</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2014 Jun 10;111(23):8446-51</Citation><ArticleIdList><ArticleId IdType="pubmed">24912171</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2000 Jan 15;8(1):79-88</Citation><ArticleIdList><ArticleId IdType="pubmed">10673428</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2011 Sep 2;333(6047):1279-82</Citation><ArticleIdList><ArticleId IdType="pubmed">21885779</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1992 Jul 1;207(1):103-7</Citation><ArticleIdList><ArticleId IdType="pubmed">1321038</ArticleId></ArticleIdList></Reference><Reference><Citation>Angew Chem Int Ed Engl. 2009;48(9):1550-74</Citation><ArticleIdList><ArticleId IdType="pubmed">19165853</ArticleId></ArticleIdList></Reference><Reference><Citation>Chem Soc Rev. 2012 Feb 7;41(3):1218-60</Citation><ArticleIdList><ArticleId IdType="pubmed">22008827</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 2011 Oct;77(19):7007-15</Citation><ArticleIdList><ArticleId IdType="pubmed">21821740</ArticleId></ArticleIdList></Reference><Reference><Citation>Biophys Chem. 2006 Sep 20;123(2-3):102-12</Citation><ArticleIdList><ArticleId IdType="pubmed">16730114</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS J. 2005 Jun;272(11):2869-77</Citation><ArticleIdList><ArticleId IdType="pubmed">15943818</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12468-72</Citation><ArticleIdList><ArticleId IdType="pubmed">11592975</ArticleId></ArticleIdList></Reference><Reference><Citation>Angew Chem Int Ed Engl. 2012 Mar 12;51(11):2628-31</Citation><ArticleIdList><ArticleId IdType="pubmed">22509501</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2016 May 27;352(6289):1098-101</Citation><ArticleIdList><ArticleId IdType="pubmed">27127235</ArticleId></ArticleIdList></Reference><Reference><Citation>ACS Chem Biol. 2011 Dec 16;6(12):1399-406</Citation><ArticleIdList><ArticleId IdType="pubmed">22004347</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1992 May 4;302(1):77-80</Citation><ArticleIdList><ArticleId IdType="pubmed">1587358</ArticleId></ArticleIdList></Reference><Reference><Citation>Enzyme Microb Technol. 2001 Feb 1;28(2-3):129-138</Citation><ArticleIdList><ArticleId IdType="pubmed">11166803</ArticleId></ArticleIdList></Reference><Reference><Citation>Dalton Trans. 2013 Dec 7;42(45):16102-7</Citation><ArticleIdList><ArticleId IdType="pubmed">24002580</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Feb 28;278(9):7160-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12493734</ArticleId></ArticleIdList></Reference><Reference><Citation>Biosci Biotechnol Biochem. 2001 Sep;65(9):2050-7</Citation><ArticleIdList><ArticleId IdType="pubmed">11676020</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2000 Nov 7;39(44):13595-601</Citation><ArticleIdList><ArticleId IdType="pubmed">11063597</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1998 Mar 3;1383(1):48-54</Citation><ArticleIdList><ArticleId IdType="pubmed">9546045</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1999 Feb 5;274(6):3338-44</Citation><ArticleIdList><ArticleId IdType="pubmed">9920875</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2011 Aug 5;333(6043):755-8</Citation><ArticleIdList><ArticleId IdType="pubmed">21817054</ArticleId></ArticleIdList></Reference><Reference><Citation>Carbohydr Res. 2017 Aug 7;448:200-204</Citation><ArticleIdList><ArticleId IdType="pubmed">28291519</ArticleId></ArticleIdList></Reference><Reference><Citation>Ultramicroscopy. 2006 Jun-Jul;106(8-9):881-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16730410</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1974 Dec 15;49(2):282-5</Citation><ArticleIdList><ArticleId IdType="pubmed">4474960</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2003 Apr 18;1604(1):47-54</Citation><ArticleIdList><ArticleId IdType="pubmed">12686420</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Commun. 2015 Jul 07;6:7542</Citation><ArticleIdList><ArticleId IdType="pubmed">26151670</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Chem Biol. 2016 Apr;12 (4):298-303</Citation><ArticleIdList><ArticleId IdType="pubmed">26928935</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioelectrochemistry. 2009 Sep;76(1-2):42-52</Citation><ArticleIdList><ArticleId IdType="pubmed">19640808</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2009 Dec 25;284(52):36186-90</Citation><ArticleIdList><ArticleId IdType="pubmed">19858200</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioresour Technol. 2011 Nov;102(21):10020-7</Citation><ArticleIdList><ArticleId IdType="pubmed">21903381</ArticleId></ArticleIdList></Reference><Reference><Citation>Chem Rev. 2014 Mar 26;114(6):3120-88</Citation><ArticleIdList><ArticleId IdType="pubmed">24476364</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2013 May 3;288(18):12828-39</Citation><ArticleIdList><ArticleId IdType="pubmed">23525113</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000146 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 000146 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Curation
|type= RBID
|clé= pubmed:28989682
|texte= Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:28989682" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |