Gutman 1972 FEBS Lett
|Gutman M, Silman N (1972) Mutual inhibition between NADH oxidase and succinoxidase activities in respiring submitochondrial particles. FEBS Lett 26:207-10. doi: 10.1016/0014-5793(72)80574-x.|
Abstract: The dehydrogenases of the respiratory system can oxidize substrates at rates much higher than the respiration rate. When more than one substrate is oxidized, the rate of respiration is less than the sum of the rates of respiration on each substrate separately [ 1-4]. In such a case, not only are the dehydrogenases partially utilized, but they also inhibit each other. This type of mutual inhibition was postulated to operate at the junction of the flavoprotein and the CoQlo , but a detailed mechanism was not proposed.
It seems that the mutual inhibition in multi-substrate respiration is a very sensitive probe which enables one to discriminate between fractions of the CoQlo pool, a property that is naturally masked when the parameter measured is the total amount of reduction. In conclusion, a hypothesis is suggested, which describes the CoQl0 to be divided into pools. Each pool is reduced by it's specific dehydrogenase and can interact, in a spill-over mechanism, with other pools. The final steady state reduction of each pool, determined by the influx and efflux of electrons, will be reflected in the rate of oxidation of the reduced dehydrogenase by the CoQlo.
• Bioblast editor: Gnaiger E
- ETPH, electron transport particle (membrane preparation)
- Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5th ed. Bioenerg Commun 2020.2. https://doi.org/10.26124/bec:2020-0002
Labels: MiParea: Respiration
Regulation: Flux control, Inhibitor, Q-junction effect
Pathway: N, S, NS