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Flavodoxin Is Required for the Activation of the Anaerobic Ribonucleotide Reductase
dc.contributor.authorBianchi, V.en_US
dc.contributor.authorEliasson, R.en_US
dc.contributor.authorFontecave, M.en_US
dc.contributor.authorMulliez, E.en_US
dc.contributor.authorHoover, D. M.en_US
dc.contributor.authorMatthews, Rowena Greenen_US
dc.contributor.authorReichard, P.en_US
dc.date.accessioned2006-05-10T15:34:10Z
dc.date.available2006-05-10T15:34:10Z
dc.date.issued1993-12-15en_US
dc.identifier.citationBianchi V., , Eliasson R., , Fontecave M., , Mulliez E., , Hoover D. M., , Matthews R. G., , Reichard P., (1993/12/15)."Flavodoxin Is Required for the Activation of the Anaerobic Ribonucleotide Reductase." Biochemical and Biophysical Research Communications 197(2): 792-797. <http://hdl.handle.net/2027.42/30392>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-45PTT7R-7P/2/89645a597c2362cb6e982b89bd5c702aen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/30392
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8267617&dopt=citationen_US
dc.description.abstractThe inactive anaerobic ribonucleotide reductase from Escherichia coli is transformed by a multienzyme system and S-adenosylmethionine + NADPH into a radical protein that is enzymatically active. One of the activating enzyme components was earlier shown to be ferredoxin (flavodoxin):NADP+ reductase. Here we present evidence that flavodoxin, but not ferredoxin, also is a component of the system. Light reduced deazaflavin can substitute for the flavodoxin system. An additional unidentified low-molecular weight component further stimulates the reaction.en_US
dc.format.extent6 bytes
dc.format.extent3118 bytes
dc.format.extent291478 bytes
dc.format.mimetypetext/plain
dc.format.mimetypetext/plain
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.titleFlavodoxin Is Required for the Activation of the Anaerobic Ribonucleotide Reductaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumUniv Michigan, Div Biophys Res, Ann Arbor, MI 48109, USA and Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationotherKarolinska Inst, Inst Med Noble, Dept Biochem 1, S 17177 Stockholm, Swedenen_US
dc.contributor.affiliationotherUniv Joseph Fourier, Etud Dynam & Struct Select Lab, F 38041 Grenoble 9, Franceen_US
dc.contributor.affiliationotherUniv Joseph Fourier, Etud Dynam & Struct Select Lab, F 38041 Grenoble 9, Franceen_US
dc.contributor.affiliationotherUniv Joseph Fourier, Etud Dynam & Struct Select Lab, F 38041 Grenoble 9, Franceen_US
dc.contributor.affiliationotherUniv Michigan, Div Biophys Res, Ann Arbor, MI 48109, USA and Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationotherKarolinska Inst, Inst Med Noble, Dept Biochem 1, S 17177 Stockholm, Swedenen_US
dc.identifier.pmid8267617en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/30392/3/0000010.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1006/bbrc.1993.2548en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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