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Resonance Raman spectroscopy of cytochrome oxidase and electron transport particles with excitation near the Soret band

dc.contributor.authorSalmeen, Irving T.en_US
dc.contributor.authorRimai, L.en_US
dc.contributor.authorGill, D.en_US
dc.contributor.authorYamamoto, Tomokoen_US
dc.contributor.authorPalmer, Grahamen_US
dc.contributor.authorHartzell, C. R.en_US
dc.contributor.authorBeinert, Helmuten_US
dc.date.accessioned2006-04-17T16:38:20Z
dc.date.available2006-04-17T16:38:20Z
dc.date.issued1973-06-08en_US
dc.identifier.citationSalmeen, I., Rimai, L., Gill, D., Yamamoto, T., Palmer, G., Hartzell, C. R., Beinert, H. (1973/06/08)."Resonance Raman spectroscopy of cytochrome oxidase and electron transport particles with excitation near the Soret band." Biochemical and Biophysical Research Communications 52(3): 1100-1107. <http://hdl.handle.net/2027.42/33860>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DYM9YK-1YM/2/93ce5626dd74d5cb939a953a8327fcdeen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33860
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4351046&dopt=citationen_US
dc.description.abstractWe report the resonance Raman spectra of cytochrome oxidase, both solubilized and in electron transport particles using laser excitation near the Soret band. As in the spectra of other hemoproteins, such as cytochrome , the shape and intensity of a number of bands change when the oxidation state is varied. However, one of the hemes of solubilized cytochrome oxidase shows redox behavior which is anomalous. Spectra of electron transport particles are dominated by cytochrome oxidase. There are, however, definite differences between spectra of solubilized cytochrome oxidase and electron transport particles in the oxidized states.en_US
dc.format.extent446801 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleResonance Raman spectroscopy of cytochrome oxidase and electron transport particles with excitation near the Soret banden_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.affiliationumBiophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, MI 48104, USAen_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, MI 48104, USAen_US
dc.contributor.affiliationotherScientific Research Staff, Ford Motor Co., Dearborn, MI 48121, USAen_US
dc.contributor.affiliationotherScientific Research Staff, Ford Motor Co., Dearborn, MI 48121, USAen_US
dc.contributor.affiliationotherScientific Research Staff, Ford Motor Co., Dearborn, MI 48121, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry, Pennsylvania State University, University Park, PA 16802, USAen_US
dc.contributor.affiliationotherInstitute for Enzyme Research, University of Wisconsin, Madison, WI 53706, USAen_US
dc.identifier.pmid4351046en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33860/1/0000121.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(73)91051-6en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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