| Autor: |
Samain, E., Patil, D.S., DerVartanian, D.V., Albagnac, G., LeGall, J. |
| Zdroj: |
FEBS Letters; May 1987, Vol. 216 Issue: 1 p140-144, 5p |
| Abstrakt: |
Succinate dehydrogenase was purified from the particulate fraction of Desulfobulbus. The enzyme catalysed both fumarate reduction and succinate oxidation but the rate of fumarate reduction was 8‐times less than that of succinate oxidation. Quantitative analysis showed the presence of 1 mol of covalently bound flavin and 1 mol of cytochrome bper mol of succinate dehydrogenase. The enzyme contained three subunits with molecular mass 68.5, 27.5 and 22 kDa. EPR spectroscopy indicated the presence of at least two iron sulfur clusters. 2‐Heptyl‐4‐hydroxy‐quinoline‐N‐oxide inhibited the electron‐transfer between succinate dehydrogenase and a high redox potential cytochrome c3from Desulfobulbus elongatus. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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