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Difference between revisions of "Beauvoit 1999 Biochim Biophys Acta"

From Bioblast
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|year=1999
|year=1999
|journal=Eur J Biochem
|journal=Eur J Biochem
|abstract=The role of the nuclear-encoded subunit VIa in the regulation of cytochrome oxidase by ATP was investigated in
|abstract=The role of the nuclear-encoded subunit VIa in the regulation of cytochrome oxidase by ATP was investigated in isolated yeast mitochondria. As the subunit VIa-null strain possesses a fully active and assembled cytochrome oxidase, multiple ATP-regulating sites were characterized with respect to their location and their kinetic effect:
isolated yeast mitochondria. As the subunit VIa-null strain possesses a fully active and assembled cytochrome
Β 
oxidase, multiple ATP-regulating sites were characterized with respect to their location and their kinetic effect:
(a) intra-mitochondrial ATP inhibited the complex IV activity of the null strain, whereas the prevailing effect of
(a) intra-mitochondrial ATP inhibited the complex IV activity of the null strain, whereas the prevailing effect of
ATP on the wild-type strain, at low ionic strength, was activation on the cytosolic side of complex IV, mediated
ATP on the wild-type strain, at low ionic strength, was activation on the cytosolic side of complex IV, mediated
Line 14: Line 13:
inhibition (null-mutant) of the cytochrome oxidase by ATP; (c) consequently, the control coefficient of
inhibition (null-mutant) of the cytochrome oxidase by ATP; (c) consequently, the control coefficient of
cytochrome oxidase on respiratory flux, decreased (wild-type) or increased (null-mutant) in the presence of ATP;
cytochrome oxidase on respiratory flux, decreased (wild-type) or increased (null-mutant) in the presence of ATP;
(d) considering electron transport from cytochrome c to oxygen, the response of cytochrome oxidase to its
(d) considering electron transport from cytochrome c to oxygen, the response of cytochrome oxidase to its thermodynamic driving force was increased by ATP for the wild-type but not for the mutant subunit. Taken together, these findings indicate that at physiological concentration, ATP regulates yeast cytochrome oxidase via subunit-mediated interactions on both sides of the inner membrane, thus subtly tuning the thermodynamic and kinetic control of respiration. This study opens up new prospects for understanding the feedback regulation of the respiratory chain by ATP.
thermodynamic driving force was increased by ATP for the wild-type but not for the mutant subunit. Taken
together, these findings indicate that at physiological concentration, ATP regulates yeast cytochrome oxidase via
subunit-mediated interactions on both sides of the inner membrane, thus subtly tuning the thermodynamic and
kinetic control of respiration. This study opens up new prospects for understanding the feedback regulation of the
respiratory chain by ATP.
|keywords=ATP regulation, Cytochrome c oxidase, Mitochondria, Saccharomyces cerevisiae, ubunit VIa.
|keywords=ATP regulation, Cytochrome c oxidase, Mitochondria, Saccharomyces cerevisiae, ubunit VIa.
|mipnetlab=FR_Bordeaux_Rigoulet M, FR_Pessac_Beauvoit B, FR Bordeaux Devin A
|mipnetlab=FR_Bordeaux_Rigoulet M, FR_Pessac_Beauvoit B, FR Bordeaux Devin A
}}
}}
{{Labeling
{{Labeling
|instruments=Oxygraph-2k
|area=Respiration
|organism=Saccharomyces cerevisiae
|organism=Saccharomyces cerevisiae
|taxonomic group=Fungi
|taxonomic group=Fungi
|preparations=Oxidase; Biochemical Oxidation
|preparations=Oxidase; Biochemical Oxidation
|enzymes=Complex IV; Cytochrome c Oxidase
|enzymes=Complex IV; Cytochrome c Oxidase
|kinetics=ADP; Pi
|topics=ADP, ATP
|instruments=Oxygraph-2k
}}
}}

Revision as of 14:59, 11 August 2013

Publications in the MiPMap
Beauvoit B, Bunoust O, GuΓ©rin B, Rigoulet M (1999) ATP-regulation of cytochrome oxidase in yeast mitochondria. Role of subunit VIa. Eur J Biochem 263: 118-127.


Beauvoit B, Bunoust O, Guerin B, Rigoulet M (1999) Eur J Biochem

Abstract: The role of the nuclear-encoded subunit VIa in the regulation of cytochrome oxidase by ATP was investigated in isolated yeast mitochondria. As the subunit VIa-null strain possesses a fully active and assembled cytochrome oxidase, multiple ATP-regulating sites were characterized with respect to their location and their kinetic effect:

(a) intra-mitochondrial ATP inhibited the complex IV activity of the null strain, whereas the prevailing effect of ATP on the wild-type strain, at low ionic strength, was activation on the cytosolic side of complex IV, mediated by subunit VIa. However, at physiological ionic strength (i.e. <200 mm), activation by ATP was absent but inhibition was not impaired; (b) in ethanol-respiring mitochondria, when the electron flux was modulated using a protonophoric uncoupler, the redox state of aa3 cytochromes varied with respect to activation (wild-type) or inhibition (null-mutant) of the cytochrome oxidase by ATP; (c) consequently, the control coefficient of cytochrome oxidase on respiratory flux, decreased (wild-type) or increased (null-mutant) in the presence of ATP; (d) considering electron transport from cytochrome c to oxygen, the response of cytochrome oxidase to its thermodynamic driving force was increased by ATP for the wild-type but not for the mutant subunit. Taken together, these findings indicate that at physiological concentration, ATP regulates yeast cytochrome oxidase via subunit-mediated interactions on both sides of the inner membrane, thus subtly tuning the thermodynamic and kinetic control of respiration. This study opens up new prospects for understanding the feedback regulation of the respiratory chain by ATP. β€’ Keywords: ATP regulation, Cytochrome c oxidase, Mitochondria, Saccharomyces cerevisiae, ubunit VIa.

β€’ O2k-Network Lab: FR_Bordeaux_Rigoulet M, FR_Pessac_Beauvoit B, FR Bordeaux Devin A


Labels: MiParea: Respiration 


Organism: Saccharomyces cerevisiae 

Preparation: Oxidase; Biochemical Oxidation"Oxidase; Biochemical Oxidation" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.  Enzyme: Complex IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.  Regulation: ADP, ATP 


HRR: Oxygraph-2k