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dc.contributor.authorSong, David Y.
dc.contributor.authorPizano, Arturo A.
dc.contributor.authorHolder, Patrick G.
dc.contributor.authorStubbe, JoAnne
dc.contributor.authorNocera, Daniel
dc.date.accessioned2017-07-20T14:43:00Z
dc.date.issued2015
dc.identifierQuick submit: 2017-05-11T12:22:16-0400
dc.identifier.citationSong, David Y., Arturo A. Pizano, Patrick G. Holder, JoAnne Stubbe, and Daniel G. Nocera. 2015. Direct Interfacial Y731 Oxidation in α2 by a Photoβ2 Subunit of E. Coli Class Ia Ribonucleotide Reductase.” Chem. Sci. 6 (8): 4519–4524. doi:10.1039/c5sc01125f.en_US
dc.identifier.issn2041-6520en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:33468941
dc.description.abstractProton-coupled electron transfer (PCET) is a fundamental mechanism important in a wide range of biological processes including the universal reaction catalysed by ribonucleotide reductases (RNRs) in making de novo, the building blocks required for DNA replication and repair. These enzymes catalyse the conversion of nucleoside diphosphates (NDPs) to deoxynucleoside diphosphates (dNDPs). In the class Ia RNRs, NDP reduction involves a tyrosyl radical mediated oxidation occurring over 35 Å across the interface of the two required subunits (β2 and α2) involving multiple PCET steps and the conserved tyrosine triad [Y356(β2)–Y731(α2)–Y730(α2)]. We report the synthesis of an active photochemical RNR (photoRNR) complex in which a Re(I)-tricarbonyl phenanthroline ([Re]) photooxidant is attached site-specifically to the Cys in the Y356C-(β2) subunit and an ionizable, 2,3,5-trifluorotyrosine (2,3,5-F3Y) is incorporated in place of Y731 in α2. This intersubunit PCET pathway is investigated by ns laser spectroscopy on [Re356]-β2:2,3,5-F3Y731-α2 in the presence of substrate, CDP, and effector, ATP. This experiment has allowed analysis of the photoinjection of a radical into α2 from β2 in the absence of the interfacial Y356 residue. The system is competent for light-dependent substrate turnover. Time-resolved emission experiments reveal an intimate dependence of the rate of radical injection on the protonation state at position Y731(α2), which in turn highlights the importance of a well-coordinated proton exit channel involving the key residues, Y356 and Y731, at the subunit interface.en_US
dc.description.sponsorshipChemistry and Chemical Biologyen_US
dc.language.isoen_USen_US
dc.publisherRoyal Society of Chemistry (RSC)en_US
dc.relation.isversionofdoi:10.1039/C5SC01125Fen_US
dash.licenseLAA
dc.titleDirect Interfacial Y731 Oxidation in α2 by a Photoβ2 Subunit of E. Coli Class Ia Ribonucleotide Reductaseen_US
dc.typeJournal Articleen_US
dc.date.updated2017-05-11T16:21:43Z
dc.description.versionVersion of Recorden_US
dc.relation.journalChem. Sci.en_US
dash.depositing.authorNocera, Daniel
dc.date.available2015
dc.date.available2017-07-20T14:43:00Z
dc.identifier.doi10.1039/C5SC01125F*
dash.contributor.affiliatedNocera, Daniel


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