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- W1993726551 abstract "An iron-sulfur (FeS) protein has been purified from beef heart mitochondria by following its EPR signal after reduction, which is characteristic of a ferredoxin-type FeS protein (gx = 1.886; gy = 1.939; gz = 2.086). The signal intensity corresponds to one unpaired spin for 4 to 5 Fe atoms. The light absorption spectrum indicates the presence of flavin. Fe, labile S, and FAD are released by acid at a ratio of approximately 4:4:1. Neither prosthetic group of the protein is reduced by NADH, NADPH, succinate, glycerol-3-phosphate or dihydroorotate. The FeS group is, however, reduced with a half-time of ∼5 msec, when the protein is mixed with an equivalent amount of electron transferring flavoprotein (ETF) of the β-oxidation cycle, prereduced with an acyl CoA dehydrogenase and a saturated fatty acyl CoA. In the presence of the two added flavoproteins the behavior of the flavin of the FeS flavoprotein could not be determined. Complexes I–III are not reduced by reduced ETF under analogous conditions. The low field EPR resonance [“center 5”, Ohnishi et al. (1972), Biochem. Biophys. Res. Commun. 46, 1631–1638] of the protein is readily observed in whole tissue, mitochondria and sonic fragments from all species we have examined. Therefore, the protein appears to be a universal constituent of mitochondrial electron transfer systems." @default.
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- W1993726551 date "1975-09-01" @default.
- W1993726551 modified "2023-09-25" @default.
- W1993726551 title "A new membrane iron-sulfur flavoprotein of the mitochondrial electron transfer system the entrance point of the fatty acyl dehydrogenation pathway?" @default.
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- W1993726551 doi "https://doi.org/10.1016/0006-291x(75)90555-0" @default.
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