Multifrequency EPR investigations into the origin of the S2-state signal at g = 4 of the O2-evolving complex
dc.contributor.author | Haddy, Alice | en_US |
dc.contributor.author | Dunham, William Richard | en_US |
dc.contributor.author | Sands, Richard H. | en_US |
dc.contributor.author | Aasa, Roland | en_US |
dc.date.accessioned | 2006-04-10T15:21:17Z | |
dc.date.available | 2006-04-10T15:21:17Z | |
dc.date.issued | 1992-01-30 | en_US |
dc.identifier.citation | Haddy, Alice, Dunham, W. Richard, Sands, Richard H., Aasa, Roland (1992/01/30)."Multifrequency EPR investigations into the origin of the S2-state signal at g = 4 of the O2-evolving complex." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1099(1): 25-34. <http://hdl.handle.net/2027.42/30241> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1S-49PT4H9-4/2/50e9a7aee61fa65c245503d201b0c1ac | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/30241 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1310873&dopt=citation | en_US |
dc.description.abstract | The low-temperature S2-state EPR signal at g = 4 from the oxygen-evolving complex (OEC) of spinach Photosystem-II-enriched membranes is examined at three frequencies, 4 GHz (S-band), 9 GHz (X-band) and 16 GHz (P-band). While no hyperfine structure is observed at 4 GHz, the signal shows little narrowing and may mask underlying hyperline structure. At 16 GHz, the signal shows g-anisotropy and a shift in g-components. The middle Kramers doublet of a near rhombic S = 1/2 system is found to be the only possible origin consistent with the frequency dependence of the signal. Computer simulations incorporating underlying hyperfine structure from an Mn monomer or dimer are employed to characterize the system. The low zero field splitting (ZFS) of D = 0.43 cm and near rhombocity of E/D = 0.25 lead to the observed X-band g value of 4.1. Treatment with F or NH3, which compete with Cl for a binding site, increases the ZFS and rhombicity of the signal. These results indicate that the origin of the OEC signal at g = 4 is either an Mn(II) monomer or a coupled Mn multimer. The likelihood of a multimer is favored over that of a monomer. | en_US |
dc.format.extent | 889738 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 | Multifrequency EPR investigations into the origin of the S2-state signal at g = 4 of the O2-evolving complex | 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, University of Michigan, Ann Arbor, MI, U.S.A.; Department of Biochemistry and Biophysics, Chalmers University of Technology, Göteborg, Sweden. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, University of Michigan, Ann Arbor, MI, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, University of Michigan, Ann Arbor, MI, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Biochemistry and Biophysics, Chalmers University of Technology, Göteborg, Sweden | en_US |
dc.identifier.pmid | 1310873 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/30241/1/0000635.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2728(92)90183-3 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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