scholarly journals Steady state kinetics of energy-dependent Ca2+ uptake in rat liver mitochondria.

1977 ◽  
Vol 252 (13) ◽  
pp. 4539-4545
Author(s):  
S M Hutson
Keyword(s):  
Steady State ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Steady State Kinetics ◽  
Energy Dependent ◽  
Kinetics Of

scholarly journals A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors

1972 ◽  
Vol 127 (2) ◽  
pp. 321-333 ◽  
Author(s):  
Peter J. F. Henderson
Keyword(s):  
Steady State ◽  
Dose Response ◽  
Significant Proportion ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
High Affinity ◽  
Mechanism Of Inhibition ◽  
Steady State Kinetics ◽  
Linear Plot ◽  
Kinetics Of

When an enzyme exhibits a high affinity for an inhibitor, the steady-state analysis of the mechanism is complicated by the non-linearity of normal dose–response plots or of reciprocal replots. It is shown here that dose–response measurements generate a linear plot of inhibitor concentration divided by degree of inhibition against velocity without inhibitor divided by velocity with inhibitor; the concentration of enzyme may be derived from the extrapolated intercept of such plots, and the mechanism of inhibition from replots of the variation of the slope with substrate concentration. The limiting cases where virtually all inhibitor molecules are bound or virtually all are free are described, together with the situation when a significant proportion of the substrate becomes bound. This type of analysis indicates that the inhibitors of oxidative phosphorylation, rutamycin and bongkrekic acid, are tightly bound to rat liver mitochondria.

scholarly journals The Steady State Maintenance of Accumulated Ca++ in Rat Liver Mitochondria

1965 ◽  
Vol 240 (6) ◽  
pp. 2712-2720
Author(s):  
Zdenek Drahota ◽  
Ernesto Carafoli ◽  
Carlo S. Rossi ◽  
Robert L. Gamble ◽  
Albert L. Lehninger
Keyword(s):  
Steady State ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria

Tracking of proton flow during transition from anaerobiosis to steady state in rat liver mitochondria

1990 ◽  
Vol 1018 (1) ◽  
pp. 77-90 ◽  
Author(s):  
Siro Luvisetto ◽  
Carmen Cola ◽  
Thomas E. Conover ◽  
Giovanni Felice Azzone
Keyword(s):  
Steady State ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria

Steady-state and pre-steady-state kinetics of the mitochondrial F(1)F(o) ATPase: is ATP synthase a reversible molecular machine?

2000 ◽  
Vol 203 (1) ◽  
pp. 41-49 ◽  
Author(s):  
A.D. Vinogradov
Keyword(s):  
Steady State ◽  
Atp Synthase ◽  
Atp Synthesis ◽  
Gamma Subunit ◽  
Change Mechanism ◽  
Steady State Kinetics ◽  
Energy Dependent ◽  
Variable Substrate ◽  
Kinetics Of ◽  
Hydrolysis Of

H(+)-ATP synthase (F(1)F(o) ATPase) catalyzes the synthesis and/or hydrolysis of ATP, and the reactions are strongly affected by all the substrates (products) in a way clearly distinct from that expected of a simple reversibly operating enzyme. Recent studies have revealed the structure of F(1), which is ideally suited for the alternating binding change mechanism, with a rotating gamma-subunit as the energy-driven coupling device. According to this mechanism ATP, ADP, inorganic phosphate (P(i)) and Mg(2+) participate in the forward and reverse overall reactions exclusively as the substrates and products. However, both F(1) and F(1)F(o) demonstrate non-trivial steady-state and pre-steady-state kinetics as a function of variable substrate (product) concentrations. Several effectors cause unidirectional inhibition or activation of the enzyme. When considered separately, the unidirectional effects of ADP, P(i), Mg(2+) and energy supply on ATP synthesis or hydrolysis may possibly be explained by very complex kinetic schemes; taken together, the results suggest that different conformational states of the enzyme operate in the ATP hydrolase and ATP synthase reactions. A possible mechanism for an energy-dependent switch between the two states of F(1)F(o) ATPase is proposed.

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