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.
D002844:Chromatium; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D010084:Oxidation-Reduction; D013696:Temperature
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins