EPR analysis of multiple forms of [4Fe–4S] 3+ clusters in HiPIPs
dc.contributor.author | Luchinat, Claudio | en_US |
dc.contributor.author | Reijerse, Eduard J. | en_US |
dc.contributor.author | Klaassen, Adri A. K. | en_US |
dc.contributor.author | Priem, Alex H. | en_US |
dc.contributor.author | Hagen, Wilfred R. | en_US |
dc.contributor.author | Dunham, William Richard | en_US |
dc.contributor.author | Capozzi, Francesco | en_US |
dc.contributor.author | Meyer, Terrance E. | en_US |
dc.date.accessioned | 2006-09-11T19:29:04Z | |
dc.date.available | 2006-09-11T19:29:04Z | |
dc.date.issued | 2005-06 | en_US |
dc.identifier.citation | Priem, Alex H.; Klaassen, Adri A. K.; Reijerse, Eduard J.; Meyer, Terrance E.; Luchinat, Claudio; Capozzi, Francesco; Dunham, William R.; Hagen, Wilfred R.; (2005). "EPR analysis of multiple forms of [4Fe–4S] 3+ clusters in HiPIPs." JBIC Journal of Biological Inorganic Chemistry 10(4): 417-424. <http://hdl.handle.net/2027.42/47867> | en_US |
dc.identifier.issn | 0949-8257 | en_US |
dc.identifier.issn | 1432-1327 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/47867 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=15889286&dopt=citation | en_US |
dc.description.abstract | The electron paramagnetic resonance (EPR) spectrum from the [4Fe–4S] 3+ cluster in several high-potential iron–sulfur proteins (HiPIPs) is complex: it is not the pattern of a single, isolated S =1/2 system. Multifrequency EPR from 9 to 130 GHz reveals that the apparent peak positions ( g values) are frequency-independent: the spectrum is dominated by the Zeeman interaction plus g -strain broadening. The spectra taken at frequencies above the X-band are increasingly sensitive to rapid-passage effects; therefore, the X-band data, which are slightly additionally broadened by dipolar interaction, were used for quantitative spectral analysis. For a single geometrical [4Fe–4S] 3+ structure the (Fe–Fe) 5+ mixed-valence dimer can be assigned in six different ways to a pair of iron ions, and this defines six valence isomers. Systematic multicomponent g -strain simulation shows that the [4Fe–4S] 3+ paramagnets in seven HiPIPs from different bacteria each consist of three to four discernible species, and these are assigned to valence isomers of the clusters. This interpretation builds on previous EPR analyzes of [4Fe–4S] 3+ model compounds, and it constitutes a high-resolution extension of the current literature model, proposed from paramagnetic NMR studies. | en_US |
dc.format.extent | 351673 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Springer-Verlag; SBIC | en_US |
dc.subject.other | LifeSciences | en_US |
dc.subject.other | Electron Paramagnetic Resonance | en_US |
dc.subject.other | Exchange | en_US |
dc.subject.other | High-potential Iron–Sulfur Protein | en_US |
dc.subject.other | Mixed Valence | en_US |
dc.title | EPR analysis of multiple forms of [4Fe–4S] 3+ clusters in HiPIPs | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC, Delft, The Netherlands | en_US |
dc.contributor.affiliationother | Department of Physical Chemistry (Solid State NMR Spectroscopy), University of Nijmegen, The Netherlands | en_US |
dc.contributor.affiliationother | Department of Molecular Spectroscopy, University of Nijmegen, The Netherlands | en_US |
dc.contributor.affiliationother | Department of Food Science, University of Bologna, Italy | en_US |
dc.contributor.affiliationother | Department of Biochemistry, University of Arizona, Tucson, AZ, USA | en_US |
dc.contributor.affiliationother | Max Planck Institute for Bioinorganic Chemistry, Mülheim, Germany | en_US |
dc.contributor.affiliationother | Centro Risonanze Magnetiche—CERM, University of Florence, Italy | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 15889286 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/47867/1/775_2005_Article_656.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/s00775-005-0656-2 | en_US |
dc.identifier.source | JBIC Journal of Biological Inorganic Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.