Komlodi 2021 BEC Q

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Komlódi T, Cardoso LHD, Doerrier C, Moore AL, Rich PR, Gnaiger E (2021) Coupling and pathway control of coenzyme Q redox state and respiration in isolated mitochondria. Bioenerg Commun 2021.3. https://doi.org/10.26124/bec:2021-0003

» Bioenerg Commun 2021.3. Open Access pdf published online 2021-11-11

Komlodi Timea, Cardoso Luiza HD, Doerrier Carolina, Moore Anthony L, Rich Peter R, Gnaiger Erich (2021) Bioenerg Commun

Abstract: BEC.png doi:10.26124/bec:2021-0003

Graphical abstract

Redox states of the mitochondrial coenzyme Q pool, which reacts with the electron transfer system, reflect the balance between (1) reducing capacities of electron flow from fuel substrates converging at the Q-junction, (2) oxidative capacities downstream of Q to O2, and (3) the load on the OXPHOS system utilizing or dissipating the protonmotive force.

A three-electrode sensor (Rich 1988; Moore et al 1988) was implemented into the NextGen-O2k to monitor continuously the redox state of CoQ2 added as a Q-mimetic simultaneously with O2 consumption. The Q-Module was optimized for high signal-to-noise ratio, minimum drift, and minimum oxygen diffusion. CoQ2 equilibrates in the same manner as Q at Complexes CI, CII and CIII. The CoQ2 redox state is monitored amperometrically with the working electrode, which is poised at CoQ2 redox peak potentials determined by cyclic voltammetry. The voltammogram also provides quality control of the Q-sensor and reveals chemical interferences.

The CoQ2 redox state and O2 consumption were measured simultaneously in isolated mouse cardiac and brain mitochondria. CoQ2 ― and by implication mitochondrial Q ― was more oxidized when O2 flux was stimulated by coupling control: when energy demand increased from LEAK to OXPHOS and electron transfer capacities in the succinate pathway. In contrast, CoQ2 was more reduced when O2 flux was stimulated by pathway-control of electron input capacities, increasing from the NADH (N)- to succinate (S)-linked pathway which converge at the Q-junction, with CI-Q-CIII and CII-Q-CIII segments, respectively. N- and S- respiratory pathway capacities were not completely additive, compatible with partitioning of Q intermediary between the solid-state and liquid-state models of supercomplex organization. The direct proportionality of CoQ2 reduction and electron input capacities through the CI-Q-CIII and CII-Q-CIII segments suggests that CoQ2 is accurately mimicking mitochondrial Q-redox changes.

Keywords: coenzyme Q CoQ, Q-junction, Q-redox state, electron transfer system ETS, ETS-reactive Q-pool Q, mitochondrial coenzyme Q mtCoQ, supercomplexed Q, free Q-pool according to the fluid-state model Qfree, cyclic voltammetry CV, high-resolution respirometry HRR, isolated mitochondria imt, mouse heart mitochondria, mouse brain mitochondria, oxygen consumption, SUIT protocols, coupling control, pathway control, NS-pathway, additivity Bioblast editor: Gnaiger E, Cardoso LHD O2k-Network Lab: AT Innsbruck Oroboros


ORCID: ORCID.png Komlodi Timea, ORCID.png Cardoso Luiza HD, ORCID.png Doerrier Carolina, Moore Anthony L, ORCID.png Rich Peter R, ORCID.png Gnaiger Erich

Video - NextGen-O2k: the Q-Module

Data availability

Original files are available Open Access at Zenodo repository: 10.5281/zenodo.4478400

Support

Template NextGen-O2k.jpg
Supported by project NextGen-O2k which has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No. 859770.

Keywords


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O2k-Manual
Mitochondrial Respiration Medium - MiR05-Kit.
2022-03-03Bioblast pdf » Versions
O2k-Manual
NextGen-O2k: Q-Module manual
2021-10-29PDF.jpg » Versions
O2k-Protocols
Laboratory protocol: isolation of mouse heart mitochondria.
2021-08-09Bioblast pdf »Versions

Preprint

Komlodi 2021 MitoFit Q

Cited by

  • Jarmuszkiewicz W, Dominiak K, Budzinska A, Wojcicki K, Galganski L (2023) Mitochondrial coenzyme Q redox homeostasis and reactive oxygen species production. - »Bioblast link«
Gnaiger 2021 Bioenerg Commun


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  • Komlodi et al (2022) Hydrogen peroxide production, mitochondrial membrane potential and the coenzyme Q redox state measured at tissue normoxia and experimental hyperoxia in heart mitochondria. MitoFit Preprints 2021 (in prep)
  • Komlódi T, Schmitt S, Zdrazilova L, Donnelly C, Zischka H, Gnaiger E. Oxygen dependence of hydrogen peroxide production in isolated mitochondria and permeabilized cells. MitoFit Preprints (in prep).


Labels: MiParea: Respiration, Instruments;methods 


Organism: Mouse  Tissue;cell: Heart, Nervous system  Preparation: Isolated mitochondria 

Regulation: Redox state, Q-junction effect  Coupling state: LEAK, OXPHOS, ET  Pathway: N, S, NS  HRR: Oxygraph-2k, NextGen-O2k, O2k-Protocol 

Additivity, SUIT-006 Q mt D071, SUIT-006 Q ce-pce D073, SUIT-031 Q mt D072, SUIT-031 Q ce-pce D074, BEC2021.5, MitoFit 2022 NADH, MitoFit 2021 AmR, Redox, O2k-Demo 

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