Difference between revisions of "Jarmuszkiewicz 2005 Biochim Biophys Acta"
| Line 4: | Line 4: | ||
|year=2005 | |year=2005 | ||
|journal=Biochim. Biophys. Acta | |journal=Biochim. Biophys. Acta | ||
|abstract=In ''Acanthamoeba castellanii'' mitochondria, the apparent affinity values of alternative oxidase for oxygen were much lower than those for cytochrome ''c'' oxidase. For unstimulated alternative oxidase, the | |abstract=In ''Acanthamoeba castellanii'' mitochondria, the apparent affinity values of alternative oxidase for oxygen were much lower than those for cytochrome ''c'' oxidase. For unstimulated alternative oxidase, the K<sub>Mox</sub> values were around 4–5 μM both in mitochondria oxidizing 1 mM external NADH or 10 mM succinate. For alternative oxidase fully stimulated by 1 mM GMP, the KKMox values were markedly different when compared to those in the absence of GMP and they varied when different respiratory substrates were oxidized (K<sub>Mox</sub> was around 1.2 μM for succinate and around 11 μM for NADH). Thus, with succinate as a reducing substrate, the activation of alternative oxidase (with GMP) resulted in the oxidation of the ubiquinone pool, and a corresponding decrease in K<sub>Mox</sub>. However, when external NADH was oxidized, the ubiquinone pool was further reduced (albeit slightly) with alternative oxidase activation, and the K<sub>Mox</sub> increased dramatically. Thus, the apparent affinity of alternative oxidase for oxygen decreased when the ubiquinone reduction level increased either by changing the activator or the respiratory substrate availability. | ||
|keywords=Mitochondria, Alternative oxidase, Oxygen affinity, GMP stimulation, ''Acanthamoeba castellanii'' | |keywords=Mitochondria, Alternative oxidase, Oxygen affinity, GMP stimulation, ''Acanthamoeba castellanii'' | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/15949985 PMID: 15949985] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/15949985 PMID: 15949985] | ||
Revision as of 13:36, 1 October 2010
| Jarmuszkiewicz W, Czarna M, Sluse FE (2005) Substrate kinetics of the Acanthamoeba castellanii alternative oxidase and the effects of GMP. Biochim. Biophys. Acta. 1708: 71-78. |
Jarmuszkiewicz W, Czarna M, Sluse FE (2005) Biochim. Biophys. Acta
Abstract: In Acanthamoeba castellanii mitochondria, the apparent affinity values of alternative oxidase for oxygen were much lower than those for cytochrome c oxidase. For unstimulated alternative oxidase, the KMox values were around 4–5 μM both in mitochondria oxidizing 1 mM external NADH or 10 mM succinate. For alternative oxidase fully stimulated by 1 mM GMP, the KKMox values were markedly different when compared to those in the absence of GMP and they varied when different respiratory substrates were oxidized (KMox was around 1.2 μM for succinate and around 11 μM for NADH). Thus, with succinate as a reducing substrate, the activation of alternative oxidase (with GMP) resulted in the oxidation of the ubiquinone pool, and a corresponding decrease in KMox. However, when external NADH was oxidized, the ubiquinone pool was further reduced (albeit slightly) with alternative oxidase activation, and the KMox increased dramatically. Thus, the apparent affinity of alternative oxidase for oxygen decreased when the ubiquinone reduction level increased either by changing the activator or the respiratory substrate availability. • Keywords: Mitochondria, Alternative oxidase, Oxygen affinity, GMP stimulation, Acanthamoeba castellanii
Labels:
Organism: Bacteria"Bacteria" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Enzyme: TCA Cycle and Matrix Dehydrogenases"TCA Cycle and Matrix Dehydrogenases" 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., Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" 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., Complex III, 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: Respiration; OXPHOS; ETS Capacity"Respiration; OXPHOS; ETS Capacity" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
HRR: Oxygraph-2k, Chemicals; Media"Chemicals; Media" is not in the list (Oxygraph-2k, TIP2k, O2k-Fluorometer, pH, NO, TPP, Ca, O2k-Spectrophotometer, O2k-Manual, O2k-Protocol, ...) of allowed values for the "Instrument and method" property.
