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A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B

dc.contributor.authorSchepler, K. L.en_US
dc.contributor.authorDunham, William Richarden_US
dc.contributor.authorSands, Richard H.en_US
dc.contributor.authorFee, James A.en_US
dc.contributor.authorAbeles, R. H.en_US
dc.date.accessioned2006-04-07T16:35:52Z
dc.date.available2006-04-07T16:35:52Z
dc.date.issued1975-08-26en_US
dc.identifier.citationSchepler, K. L., Dunham, W. R., Sands, R. H., Fee, J. A., Abeles, R. H. (1975/08/26)."A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B." Biochimica et Biophysica Acta (BBA) - Enzymology 397(2): 510-518. <http://hdl.handle.net/2027.42/22002>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73GH-47T1W8P-JF/2/2cc4cc1dc16117793d0014f1bea83c10en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/22002
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=168925&dopt=citationen_US
dc.description.abstractWe have proposed that the "doublet" EPR spectra observed during catalysis by a number of coenzyme B1,2-requiring enzymes arises from a weak electrostatic exchange interaction between an organic free radical and low spin Co(II), B1,2r. By varying the magnitude of the exchange coupling we have quite accurately simulateed the published EPR spectra from the enzyme systems: diol dehydrase, glycerol dehydrase, ribonucleotide reductase, and ethanolamine ammonia lyase. A dipolar model was shown to be incompatible with the observed properties of these systems.en_US
dc.format.extent521064 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleA physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme Ben_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A.en_US
dc.contributor.affiliationumBiophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A.en_US
dc.contributor.affiliationumBiophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A.en_US
dc.contributor.affiliationumBiophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A.en_US
dc.contributor.affiliationumBiophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A.en_US
dc.identifier.pmid168925en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/22002/1/0000415.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2744(75)90141-2en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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