The number of Fe atoms in the iron-sulphur centers of the respiratory chain.
1. From the 57Fe hyperfine interaction in EPR spectra of reduced submitochondrial particles from the yeast Candida utilis, grown with 57Fe, it is concluded that all Fe-S centers in these particles detectable in spectra at 35-80 K are [2Fe-2S]2-(2-; 3-) centers. These are the centers 1 of NADH and succinate dehydrogenase, the Rieske Fe-S center and possibly center 2 of succinate dehydrogenase. 2. The signals of the reduced particles detectable only at temperatures below 20 K are [4Fe-4S]2-(2-; 3-) clusters. These are the centers 2,3 and 4 of NADH dehydrogenase. 3. EPR spectra of the [2Fe-2S]3- centers of Complex I and II, but not that of Complex III, display a great inequality of the Fe nuclei in the effective hyperfine interaction in the x-y direction.
D002175:Candida / Q000032:analysis; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D007501:Iron / Q000032:analysis*; D007506:Iron-Sulfur Proteins / Q000032:analysis*; D008667:Metalloproteins / Q000032:analysis*; D008928:Mitochondria / Q000032:analysis* / Q000201:enzymology; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis*; D010084:Oxidation-Reduction; D013057:Spectrum Analysis; D013385:Succinate Dehydrogenase / Q000032:analysis*
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D007501:Iron; D013385:Succinate Dehydrogenase; D009247:NADH, NADPH Oxidoreductases