Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase
dc.contributor.author | Dunham, William Richard | en_US |
dc.contributor.author | Sands, Richard H. | en_US |
dc.contributor.author | Shaw, Robert W. | en_US |
dc.contributor.author | Beinert, Helmut | en_US |
dc.date.accessioned | 2006-04-07T18:37:46Z | |
dc.date.available | 2006-04-07T18:37:46Z | |
dc.date.issued | 1983-10-17 | en_US |
dc.identifier.citation | Dunham, William R., Sands, Richard H., Shaw, Robert W., Beinert, Helmut (1983/10/17)."Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 748(1): 73-85. <http://hdl.handle.net/2027.42/25085> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T21-47RSC8J-8N/2/2ef551501fe7e764dd3dbaee56698e6b | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/25085 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6311273&dopt=citation | en_US |
dc.description.abstract | Bovine heart mitochondrial cytochrome c oxidase (cytochrome aa3) (EC 1.9.3.1) has been demonstrated to occur in several forms when the redox centers in the protein are thought to be fully oxidized. We report here the results of extensive EPR studies at 3, 8.9, 9.2, 9.4, 15 and 34 GHz on the resting state, the alternative resting state (with g = 12 at 9 GHz) and pulsed state (with g = 5 signal at 9 GHz). Theoretical consideration is given to all binary spin-coupling possibilities under the constraint that the iron atoms are either ferric or ferrous and the copper atoms are either cupric or cuprous. We conclude that the g = 12 signal can arise from any spin system with S > 1 and |D| = 0.15 cm-1. The g = 5 signals originate from an excited, integer-spin system with |D| = 0.035 cm-1, which is approximately 7 cm-1 above the ground state (not observed in EPR). It is pointed out that in interpretations of data and elaboration of suitable models in this field, the implications of spin-coupling should be considered in a comprehensive and not in a selective way. At 3 GHz, EPR spectra of CuA in the resting, pulsed and anaerobically oxidized states show that this center is identical in its EPR for all three states. | en_US |
dc.format.extent | 973894 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationother | Institute for Enzyme Research, University of Wisconsin, Madison, WI 53706, U.S.A. | en_US |
dc.contributor.affiliationother | Institute for Enzyme Research, University of Wisconsin, Madison, WI 53706, U.S.A. | en_US |
dc.identifier.pmid | 6311273 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/25085/1/0000516.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0167-4838(83)90029-8 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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