Source:http://linkedlifedata.com/resource/pubmed/id/10631604
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2000-2-8
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pubmed:abstractText |
Mössbauer spectra of the oxidized [Fe4S4]3+ and the reduced [Fe4S4]2+ clusters in the high-potential iron protein I from Ectothiorhodospira halophila were measured in a temperature range from 5 K to 240 K. EPR measurements and 57Fe electron-nuclear double resonance (ENDOR) experiments were carried out with the oxidized protein. In the oxidized state the cluster has a net spin S = 1/2 and is paramagnetic. As common in [Fe4S4]3+ clusters, the Mössbauer spectrum was simulated with two species contributing equally to the absorption area: two Fe3+ atoms couple to the "ferric-ferric" pair, and one Fe2+ and one Fe3+ atom give the "ferric-ferrous pair". For the simulation of the Mössbauer spectrum, g-values were taken from EPR measurements. A-tensor components were determined by 57Fe ENDOR experiments that turned out to be a necessary source of estimating parameters independently. In order to obtain a detailed agreement of Mössbauer and ENDOR data, electronic relaxation has to be taken into account. Relaxing the symmetry condition in a way that the electric field gradient tensor does not coincide with g- and A-tensors yielded an even better agreement of experimental and theoretical Mössbauer spectra. Spin-spin and spinlattice relaxation times were estimated by pulsed EPR; the former turned out to be the dominating mechanism at T = 5 K. Relaxation times measured by pulsed EPR and obtained from the Mössbauer fit were compared and yield nearly identical values. The reduced cluster has one additional electron and has a diamagnetic (S = 0) ground state. All the four irons are indistinguishable in the Mössbauer spectrum, indicating a mixed-valence state of Fe2.5+ for each.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/high potential iron-sulfur protein
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0949-8257
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
727-41
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10631604-Bacterial Proteins,
pubmed-meshheading:10631604-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:10631604-Halorhodospira halophila,
pubmed-meshheading:10631604-Iron-Sulfur Proteins,
pubmed-meshheading:10631604-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:10631604-Protein Conformation,
pubmed-meshheading:10631604-Recombinant Proteins,
pubmed-meshheading:10631604-Spectroscopy, Mossbauer
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pubmed:year |
1999
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pubmed:articleTitle |
Simultaneous interpretation of Mössbauer, EPR and 57Fe ENDOR spectra of the [Fe4S4] cluster in the high-potential iron protein I from Ectothiorhodospira halophila.
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pubmed:affiliation |
Physik-Department E17, Technische Universität München, Garching, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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