AbstractWe have shown that the rate of NADH-coenzyme Q reductase in rat liver mitochondria, assayed using the decyl-ubiquinone analog DB, is underevaluated, probably as a result of its low water solubility. In view of drawbacks encountered using other more soluble acceptors in this system, we demonstrate that the most reliable assay of the physiological rate of CoQ reduction by Complex I is the indirect calculation from the total rate of NADH oxidation and the rate of ubiquinol oxidation, using the pool equation of Kröger and Klingenberg [(1973) Eur. J. Biochem. 34, 358–368]
AbstractAlkaline incubation of NADH results in the formation of a very potent inhibitor of complex I...
AbstractUbiquinol:cytochrome c oxidoreductase, bc1 complex, is the enzyme in the respiratory chain o...
AbstractThe impact of complex II (succinate:ubiquinone oxidoreductase) on the mitochondrial producti...
AbstractWe have shown that the rate of NADH-coenzyme Q reductase in rat liver mitochondria, assayed ...
AbstractThe assay of Complex I activity requires the use of artificial acceptors, such as short-chai...
AbstractThe saturation kinetics of NADH and succinate oxidation for Coenzyme Q (CoQ) has been re-inv...
AbstractTightly coupled bovine heart submitochondrial particles treated to activate complex I and to...
AbstractThis review considers the interaction of Complex I with different redox acceptors, mainly ho...
The fluorescent probe erythrosine 5'-iodoacetamide (ER) binds to mitochondrial NADH-CoQ reductase (C...
AbstractThe properties of coenzymes Q (CoQ9 and CoQ10) are closely linked to their redox state (CoQo...
We report the first detailed study on the ubiquinone (coenzyme Q; abbreviated to Q) analogue specifi...
Coenzyme Q (CoQ) is an essential cofactor, primarily found in the mitochondrial inner membrane where...
AbstractThe fluorescent probe erythrosine 5′-iodoacetamide (ER) binds to mitochondrial NADH-CoQ redu...
AbstractThe quantitative data on the binding affinity of NADH, NAD+, and their analogues for complex...
AbstractTriton X-100 inhibits the NADH oxidase and rotenone-sensitive NADH-Q1 reductase activities o...
AbstractAlkaline incubation of NADH results in the formation of a very potent inhibitor of complex I...
AbstractUbiquinol:cytochrome c oxidoreductase, bc1 complex, is the enzyme in the respiratory chain o...
AbstractThe impact of complex II (succinate:ubiquinone oxidoreductase) on the mitochondrial producti...
AbstractWe have shown that the rate of NADH-coenzyme Q reductase in rat liver mitochondria, assayed ...
AbstractThe assay of Complex I activity requires the use of artificial acceptors, such as short-chai...
AbstractThe saturation kinetics of NADH and succinate oxidation for Coenzyme Q (CoQ) has been re-inv...
AbstractTightly coupled bovine heart submitochondrial particles treated to activate complex I and to...
AbstractThis review considers the interaction of Complex I with different redox acceptors, mainly ho...
The fluorescent probe erythrosine 5'-iodoacetamide (ER) binds to mitochondrial NADH-CoQ reductase (C...
AbstractThe properties of coenzymes Q (CoQ9 and CoQ10) are closely linked to their redox state (CoQo...
We report the first detailed study on the ubiquinone (coenzyme Q; abbreviated to Q) analogue specifi...
Coenzyme Q (CoQ) is an essential cofactor, primarily found in the mitochondrial inner membrane where...
AbstractThe fluorescent probe erythrosine 5′-iodoacetamide (ER) binds to mitochondrial NADH-CoQ redu...
AbstractThe quantitative data on the binding affinity of NADH, NAD+, and their analogues for complex...
AbstractTriton X-100 inhibits the NADH oxidase and rotenone-sensitive NADH-Q1 reductase activities o...
AbstractAlkaline incubation of NADH results in the formation of a very potent inhibitor of complex I...
AbstractUbiquinol:cytochrome c oxidoreductase, bc1 complex, is the enzyme in the respiratory chain o...
AbstractThe impact of complex II (succinate:ubiquinone oxidoreductase) on the mitochondrial producti...