Electron paramagnetic resonance determination of a low-lying excited state in Chromatium vinosum high-potential iron protein

The temperature dependence of the EPR spectrum of oxidized high-potential iron protein from Chromatium vinosum has been studied. From line width and intensity measurements it is possible to determine the position of the first excited unoccupied state, 160 +/- 10 cm-1 above the ground state orbital.

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Bibliographic Details
Published inBiophysical journal Vol. 20; no. 1; pp. 23 - 31
Main Authors Blum, H., Salerno, J.C., Prince, R.C., Leigh, J.S., Ohnishi, T.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.10.1977
Subjects
Chromatium
Electron Spin Resonance Spectroscopy
Iron-Sulfur Proteins
Metalloproteins
Oxidation-Reduction
Temperature
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Summary:The temperature dependence of the EPR spectrum of oxidized high-potential iron protein from Chromatium vinosum has been studied. From line width and intensity measurements it is possible to determine the position of the first excited unoccupied state, 160 +/- 10 cm-1 above the ground state orbital.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(77)85534-3