An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase.
Identifieur interne : 001224 ( PubMed/Corpus ); précédent : 001223; suivant : 001225An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase.
Auteurs : Emily Golden ; Li-Juan Yu ; Flora Meilleur ; Matthew P. Blakeley ; Anthony P. Duff ; Amir Karton ; Alice VrielinkSource :
- Scientific reports [ 2045-2322 ] ; 2017.
Abstract
The protein microenvironment surrounding the flavin cofactor in flavoenzymes is key to the efficiency and diversity of reactions catalysed by this class of enzymes. X-ray diffraction structures of oxidoreductase flavoenzymes have revealed recurrent features which facilitate catalysis, such as a hydrogen bond between a main chain nitrogen atom and the flavin redox center (N5). A neutron diffraction study of cholesterol oxidase has revealed an unusual elongated main chain nitrogen to hydrogen bond distance positioning the hydrogen atom towards the flavin N5 reactive center. Investigation of the structural features which could cause such an unusual occurrence revealed a positively charged lysine side chain, conserved in other flavin mediated oxidoreductases, in a second shell away from the FAD cofactor acting to polarize the peptide bond through interaction with the carbonyl oxygen atom. Double-hybrid density functional theory calculations confirm that this electrostatic arrangement affects the N-H bond length in the region of the flavin reactive center. We propose a novel second-order partial-charge interaction network which enables the correct orientation of the hydride receiving orbital of N5. The implications of these observations for flavin mediated redox chemistry are discussed.
DOI: 10.1038/srep40517
PubMed: 28098177
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Blakeley</name><affiliation><nlm:affiliation>Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38000, France.</nlm:affiliation></affiliation></author><author><name sortKey="Duff, Anthony P" sort="Duff, Anthony P" uniqKey="Duff A" first="Anthony P" last="Duff">Anthony P. Duff</name><affiliation><nlm:affiliation>Bragg Institute, Australian Nuclear Science and Technology Organisation, Lucas Heights NSW, 2234, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Karton, Amir" sort="Karton, Amir" uniqKey="Karton A" first="Amir" last="Karton">Amir Karton</name><affiliation><nlm:affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Vrielink, Alice" sort="Vrielink, Alice" uniqKey="Vrielink A" first="Alice" last="Vrielink">Alice Vrielink</name><affiliation><nlm:affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28098177</idno><idno type="pmid">28098177</idno><idno type="doi">10.1038/srep40517</idno><idno type="wicri:Area/PubMed/Corpus">001224</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001224</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase.</title><author><name sortKey="Golden, Emily" sort="Golden, Emily" uniqKey="Golden E" first="Emily" last="Golden">Emily Golden</name><affiliation><nlm:affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Yu, Li Juan" sort="Yu, Li Juan" uniqKey="Yu L" first="Li-Juan" last="Yu">Li-Juan Yu</name><affiliation><nlm:affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Meilleur, Flora" sort="Meilleur, Flora" uniqKey="Meilleur F" first="Flora" last="Meilleur">Flora Meilleur</name><affiliation><nlm:affiliation>Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Blakeley, Matthew P" sort="Blakeley, Matthew P" uniqKey="Blakeley M" first="Matthew P" last="Blakeley">Matthew P. Blakeley</name><affiliation><nlm:affiliation>Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38000, France.</nlm:affiliation></affiliation></author><author><name sortKey="Duff, Anthony P" sort="Duff, Anthony P" uniqKey="Duff A" first="Anthony P" last="Duff">Anthony P. Duff</name><affiliation><nlm:affiliation>Bragg Institute, Australian Nuclear Science and Technology Organisation, Lucas Heights NSW, 2234, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Karton, Amir" sort="Karton, Amir" uniqKey="Karton A" first="Amir" last="Karton">Amir Karton</name><affiliation><nlm:affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Vrielink, Alice" sort="Vrielink, Alice" uniqKey="Vrielink A" first="Alice" last="Vrielink">Alice Vrielink</name><affiliation><nlm:affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</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">The protein microenvironment surrounding the flavin cofactor in flavoenzymes is key to the efficiency and diversity of reactions catalysed by this class of enzymes. X-ray diffraction structures of oxidoreductase flavoenzymes have revealed recurrent features which facilitate catalysis, such as a hydrogen bond between a main chain nitrogen atom and the flavin redox center (N5). A neutron diffraction study of cholesterol oxidase has revealed an unusual elongated main chain nitrogen to hydrogen bond distance positioning the hydrogen atom towards the flavin N5 reactive center. Investigation of the structural features which could cause such an unusual occurrence revealed a positively charged lysine side chain, conserved in other flavin mediated oxidoreductases, in a second shell away from the FAD cofactor acting to polarize the peptide bond through interaction with the carbonyl oxygen atom. Double-hybrid density functional theory calculations confirm that this electrostatic arrangement affects the N-H bond length in the region of the flavin reactive center. We propose a novel second-order partial-charge interaction network which enables the correct orientation of the hydride receiving orbital of N5. The implications of these observations for flavin mediated redox chemistry are discussed.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">28098177</PMID><DateCreated><Year>2017</Year><Month>01</Month><Day>18</Day></DateCreated><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><PubDate><Year>2017</Year><Month>Jan</Month><Day>18</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase.</ArticleTitle><Pagination><MedlinePgn>40517</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/srep40517</ELocationID><Abstract><AbstractText>The protein microenvironment surrounding the flavin cofactor in flavoenzymes is key to the efficiency and diversity of reactions catalysed by this class of enzymes. X-ray diffraction structures of oxidoreductase flavoenzymes have revealed recurrent features which facilitate catalysis, such as a hydrogen bond between a main chain nitrogen atom and the flavin redox center (N5). A neutron diffraction study of cholesterol oxidase has revealed an unusual elongated main chain nitrogen to hydrogen bond distance positioning the hydrogen atom towards the flavin N5 reactive center. Investigation of the structural features which could cause such an unusual occurrence revealed a positively charged lysine side chain, conserved in other flavin mediated oxidoreductases, in a second shell away from the FAD cofactor acting to polarize the peptide bond through interaction with the carbonyl oxygen atom. Double-hybrid density functional theory calculations confirm that this electrostatic arrangement affects the N-H bond length in the region of the flavin reactive center. We propose a novel second-order partial-charge interaction network which enables the correct orientation of the hydride receiving orbital of N5. The implications of these observations for flavin mediated redox chemistry are discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Golden</LastName><ForeName>Emily</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Li-Juan</ForeName><Initials>LJ</Initials><AffiliationInfo><Affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meilleur</LastName><ForeName>Flora</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, United States of America.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Structural and Molecular Biochemistry, North Carolina State University, Raleigh, NC 27695, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Blakeley</LastName><ForeName>Matthew P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38000, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Duff</LastName><ForeName>Anthony P</ForeName><Initials>AP</Initials><AffiliationInfo><Affiliation>Bragg Institute, Australian Nuclear Science and Technology Organisation, Lucas Heights NSW, 2234, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Karton</LastName><ForeName>Amir</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vrielink</LastName><ForeName>Alice</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>School of Chemistry and Biochemistry, University of Western Australia, Crawley, Western Australia, 6009 Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>01</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2014 Jan 23;9(1):e86651</RefSource><PMID Version="1">24466188</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2011 May 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