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Theoretical analysis of a temperature-dependent model of respiratory O₂ consumption using the kinetics of the cytochrome and alternative pathways.

ABSTRACT: Temperature dependence of plant respiratory O₂ -consumption has been empirically described by the Arrhenius equation. The slope of the Arrhenius plot (which is proportional to activation energy) sometimes deviates from a constant value. We conducted kinetic model simulations of mitochondrial electron flow dynamics to clarify factors affecting the shape of the Arrhenius plot. We constructed a kinetic model of respiration in which competitive O₂ -consumption by the cytochrome pathway (CP) and the alternative pathway (AP) were considered, and we used this model to describe the temperature dependence of respiratory O₂ -consumption of Arabidopsis. The model indicated that the electron partitioning and activation energy differences between CP and AP were reflected in the slope and magnitude of the dependent variables of the Arrhenius plot. When the electron partitioning and activation energies of CP and AP were constant with temperature change, our model suggested that the Arrhenius plot would be almost linear. When the electron partitioning or activation energy of CP, or both, rapidly changed with temperature, the Arrhenius plot deviated from linearity, as reported in previous experimental studies. Our simulation analysis quantitatively linked the kinetic model parameters with physiological mechanisms underlying the instantaneous temperature dependence of plant respiration rate.

SUBMITTER: Inoue T

PROVIDER: S-EPMC7821261 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Theoretical analysis of a temperature-dependent model of respiratory O2 consumption using the kinetics of the cytochrome and alternative pathways.

Inoue Tomomi T Noguchi Ko K

The New phytologist 20201025 3

Temperature dependence of plant respiratory O2 -consumption has been empirically described by the Arrhenius equation. The slope of the Arrhenius plot (which is proportional to activation energy) sometimes deviates from a constant value. We conducted kinetic model simulations of mitochondrial electron flow dynamics to clarify factors affecting the shape of the Arrhenius plot. We constructed a kinetic model of respiration in which competitive O2 -consumption by the cytochrome ...[more]

PMID: 32984969

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Project description:Bacterial alternative complex III (ACIII) catalyzes menaquinol (MKH2) oxidation, presumably fulfilling the role of cytochromes bc1/b6f in organisms that lack these enzymes. The molecular mechanism of ACIII is unknown and so far the complex has remained inaccessible for genetic modifications. The recently solved cryo-electron microscopy (cryo-EM) structures of ACIII from Flavobacterium johnsoniae, Rhodothermus marinus, and Roseiflexus castenholzii revealed no structural similarity to cytochrome bc1/b6f and there were variations in the heme-containing subunits ActA and ActE. These data implicated intriguing alternative electron transfer paths connecting ACIII with its redox partner, and left the contributions of ActE and the terminal domain of ActA to the catalytic mechanism unclear. Here, we report genetic deletion and complementation of F. johnsoniae actA and actE and the functional implications of such modifications. Deletion of actA led to the loss of activity of cytochrome aa3 (a redox partner of ACIII in this bacterium), which confirmed that ACIII is the sole source of electrons for this complex. Deletion of actE did not impair the activity of cytochrome aa3, revealing that ActE is not required for electron transfer between ACIII and cytochrome aa3. Nevertheless, absence of ActE negatively impacted the cell growth rate, pointing toward another, yet unidentified, function of this subunit. Possible explanations for these observations, including a proposal of a split in electron paths at the ActA/ActE interface, are discussed. The described system for genetic manipulations in F. johnsoniae ACIII offers new tools for studying the molecular mechanism of operation of this enzyme. IMPORTANCE Energy conversion is a fundamental process of all organisms, realized by specialized protein complexes, one of which is alternative complex III (ACIII). ACIII is a functional analogue of well-known mitochondrial complex III, but operates according to a different, still unknown mechanism. To understand how ACIII interacts functionally with its protein partners, we developed a genetic system to mutate the Flavobacterium johnsoniae genes encoding ACIII subunits. Deletion and complementation of heme-containing subunits revealed that ACIII is the sole source of electrons for cytochrome aa3 and that one of the redox-active subunits (ActE) is dispensable for electron transfer between these complexes. This study sheds light on the operation of the supercomplex of ACIII and cytochrome aa3 and suggests a division in the electron path within ACIII. It also shows a way to manipulate protein expression levels for application in other members of the Bacteroidetes phylum.

Dataset Information

Theoretical analysis of a temperature-dependent model of respiratory O₂ consumption using the kinetics of the cytochrome and alternative pathways.

Publications

Theoretical analysis of a temperature-dependent model of respiratory O<sub>2</sub> consumption using the kinetics of the cytochrome and alternative pathways.

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