Abstract
Regulation of succinate dehydrogenase was investigated using tightly coupled potato tuber mitochondria in a novel fashion by simultaneously measuring the oxygen uptake rate and the ubiquinone (Q) reduction level. We found that the activation level of the enzyme is unambiguously reflected by the kinetic dependence of the succinate oxidation rate upon the Q-redox poise. Kinetic results indicated that succinate dehydrogenase is activated by both ATP (K
Original language | English |
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Pages (from-to) | 32567-32574 |
Journal | Journal of Biological Chemistry |
Volume | 276 |
DOIs | |
Publication status | Published - 2001 |