Relationships of respiratory chain and ATP-synthetase in energized mitochondria.
The present study reveals that the previously described effect of ATP-synthetase inhibition concomitant with inhibition of respiratory chain functioning may be observed at different absolute values of delta psi on the mitochondrial membrane. This fact points out that the membrane potential is not a unique regulator in coupling of ATP-synthetase and respiratory chain activities. We found, using the double-inhibitor titration technique, that ATP-synthetase inhibition induces proportional inhibition of respiratory chain enzymes and vice versa respiratory chain inhibition induces proportional inhibition of ATP-synthetase. This effect is shown to exist only when osmolarity is close to 150-300 (mosM) (in the physiological range). The coupling effectivity (ADP/O) of mitochondria under these conditions is maximal. Under conditions of high osmolarity (400-600 mosM) the respiratory chain and ATP-synthetase behave as if they were coupled by bulk phase delta -mu H+, from the kinetic point of view.
D025181:ATP Synthetase Complexes; D000818:Animals; D008930:Mitochondria, Liver / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009994:Osmolar Concentration; D010101:Oxygen Consumption; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D051381:Rats
D009097:Multienzyme Complexes; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes