Comments on the g tensor variations in selenium-substituted 2Fe-2S iron-sulfur proteins.
The representation of the g values, gx, gy, gz, of reduced selenium-substituted 2Fe-2S ferredoxins as a function of the difference gy--gx, shows a correlation which is similar to that observed in the case of the native proteins. For these proteins, a model was presented in a previous work (Bertrand, P. and Gayda, J.P. (1979) Biochim. Biophys. Acta 579, 107--121) in which this correlation was explained on the basis of a variable rhombic distortion at the Fe(II) site. It is shown here that the same interpretation holds for the selenium derivatives. A good agreement with the experimental data is obtained by choosing for the g values of Fe(III) the values measured for the Fe(III)Se2S2 clusters in ZnS crystals.
D000311:Adrenal Glands; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005288:Ferredoxins; D005290:Ferric Compounds; D019684:Magnoliopsida; D008956:Models, Chemical; D011549:Pseudomonas; D012643:Selenium; D013455:Sulfur; D013552:Swine
D005288:Ferredoxins; D005290:Ferric Compounds; D013455:Sulfur; D012643:Selenium