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Dual-mode EPR spectrometry of O2-pulsed cytochrome c oxidase
dc.contributor.authorHagen, Wilfred R.en_US
dc.contributor.authorDunham, William Richarden_US
dc.contributor.authorSands, Richard H.en_US
dc.contributor.authorShaw, Robert W.en_US
dc.contributor.authorBeinert, Helmuten_US
dc.date.accessioned2006-04-07T18:26:29Z
dc.date.available2006-04-07T18:26:29Z
dc.date.issued1984-06-26en_US
dc.identifier.citationHagen, Wilfred R., Dunham, William R., Sands, Richard H., Shaw, Robert W., Beinert, Helmut (1984/06/26)."Dual-mode EPR spectrometry of O2-pulsed cytochrome c oxidase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 765(3): 399-402. <http://hdl.handle.net/2027.42/24775>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1S-47RB89X-3P/2/d200a6df8cf76cbe9c8d0f3c50ca364cen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/24775
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6329275&dopt=citationen_US
dc.description.abstractO2-activated bovine heart cytochrome c oxidase has been examined by dual-mode EPR spectrometry. Resonances have been observed at g = 10 and 4.5 in the parallel mode and at g = 10, 5, 1.8 and 1.7 in the normal mode. The bulk of these signals are interpreted to come from a stoichiometric S = 2 system with |a| = 0.17 cm-1, D = +2.1 cm-1, |E| = 0.026 cm-, g = 2. Exchange coupling between cytochrome a3 and CuB is not indicated.en_US
dc.format.extent281296 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleDual-mode EPR spectrometry of O2-pulsed cytochrome c oxidaseen_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.affiliationumBiophysics Research Division, Institute of Science and Technology, The University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology, The University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology, The University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationotherChemistry Department, Texas Tech University, Lubbock, TX 79409, U.S.A.en_US
dc.contributor.affiliationotherInstitute for Enzyme Research and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, WI 53706, U.S.A.en_US
dc.identifier.pmid6329275en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/24775/1/0000199.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2728(84)90181-6en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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