Characterization of the multiple EPR line shapes of iron-semiquinones in photosystem 2.
We have compared the temperature-dependence characteristics of the EPR signals of Qa and Qb iron-semiquinones from both purple bacterial and plant photosystems. The data obtained were analyzed and estimates of the splitting parameters of the non-heme Fe2+ spin sublevels obtained. The study confirms the similarities of the g = 1.8 Qa iron-semiquinone signal (D/k = 15.6 K, E/k = 3.3 K) formed in formate-treated plant photosystem 2 to the signal found in purple bacteria. However, the g = 1.9 Qa iron-semiquinone signal (D/k = 7.1 K, E/k = much less than 1 K), formed in photosystem 2 when bicarbonate remains bound, has a unique temperature behavior. A series of spectral features associated with the iron-semiquinone in bicarbonate-bound photosystem 2 appear as the temperature is lowered, and the analysis of these data requires that some of these features be assigned to the higher spin states. The results are discussed in terms of the requirement for bicarbonate to be a ligand of the non-heme iron.
Nugent
J H
JH
Department of Biology, University College London, United Kingdom.
Doetschman
D C
DC
Maclachlan
D J
DJ
D016227:Benzoquinones / Q000378:metabolism*; D001639:Bicarbonates / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism; D000458:Cyanobacteria / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D007425:Intracellular Membranes / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism; D012241:Rhodopseudomonas / Q000378:metabolism; D013696:Temperature
D016227:Benzoquinones; D001639:Bicarbonates; D045322:Photosynthetic Reaction Center Complex Proteins; C025232:semiquinone radicals; D007501:Iron