Difference between revisions of "Talk:Komlodi 2021 MitoFit Q"
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|year=2021-02-15 | |year=2021-02-15 | ||
|journal=MitoFit Prep | |journal=MitoFit Prep | ||
|abstract= | |abstract= Redox states of mitochondrial coenzyme Q (mtCoQ or Q) 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 oxygen, 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 the Q redox state continuously and simultaneously with oxygen consumption. The Q-Module was optimized for high signal-to-noise ratio and minimum oxygen diffusion. CoQ2 is added as a redox probe equilibrating with Q at Complexes CI, CII and CIII and the detecting electrode. Q-sensors are poised with the CoQ2 redox peak potentials determined by cyclic voltammetry, which provides quality control of the Q-sensor and reveals chemical interferences. | ||
|keywords= | The Q redox state and oxygen consumption were measured simultaneously in isolated mitochondria. A coupling-control protocol was applied to analyze LEAK, OXPHOS, and electron transfer capacities (L, P, and E, respectively) in the succinate-pathway. In a second pathway-control protocol, NADH- and succinate-linked pathways (N and S) converge at the Q-junction. mtCoQ was more oxidized when O2 flux was stimulated in coupling-control states with load increasing from L to P and E. In contrast, mtCoQ was more reduced when O2 flux was stimulated with electron input capacities increasing from N-, S- to NS-pathway-control states. N- and S- pathway capacities were not completely additive, thus confirming partial pool behavior of Q as proposed in the plasticity model of supercomplex organization. | ||
|keywords=Q-junction, mitochondria, oxygen consumption, Q redox state, three-electrode system, cyclic voltammetry, harmonized SUIT protocols, high-resolution respirometry, coupling control, pathway control, NS-pathway, additivity | |||
|editor= | |editor= | ||
|mipnetlab=AT Innsbruck Oroboros | |mipnetlab=AT Innsbruck Oroboros | ||
}} | }} | ||
ORC'''ID''': [[File:ORCID.png|20px|link=https://orcid.org/0000-0001-9876-1411]] Komlodi Timea, [[File:ORCID.png|20px|link=https://orcid.org/0000-0001-6392-9229]] Cardoso Luiza HD, [[File:ORCID.png|20px|link=https://orcid.org/0000-0002-7969-6762]] Doerrier Carolina, [[File:ORCID.png|20px|link=https://orcid.org/0000-0003-3647-5895]] Gnaiger Erich | ORC'''ID''': [[File:ORCID.png|20px|link=https://orcid.org/0000-0001-9876-1411]] Komlodi Timea, [[File:ORCID.png|20px|link=https://orcid.org/0000-0001-6392-9229]] Cardoso Luiza HD, [[File:ORCID.png|20px|link=https://orcid.org/0000-0002-7969-6762]] Doerrier Carolina, [[File:ORCID.png|20px|link=https://orcid.org/0000-0003-3647-5895]] Gnaiger Erich | ||
Revision as of 16:57, 18 February 2021
Talk:Komlodi 2021 MitoFit Q
| Komlodi T, Cardoso LHD, Doerrier C, Gnaiger E (2021) Coupling and pathway control of coenzyme Q redox state and respiration in isolated mitochondria. MitoFit Preprints 2021.2. doi:10.26124/mitofit:2021-0002 |
»
Simultaneous measurement of respiration and redox state of coenzyme Q in isolated mitochondria
Komlodi Timea, Cardoso Luiza HD, Doerrier Carolina, Gnaiger Erich (2021-02-15) MitoFit Prep
Abstract: Redox states of mitochondrial coenzyme Q (mtCoQ or Q) 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 oxygen, 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 the Q redox state continuously and simultaneously with oxygen consumption. The Q-Module was optimized for high signal-to-noise ratio and minimum oxygen diffusion. CoQ2 is added as a redox probe equilibrating with Q at Complexes CI, CII and CIII and the detecting electrode. Q-sensors are poised with the CoQ2 redox peak potentials determined by cyclic voltammetry, which provides quality control of the Q-sensor and reveals chemical interferences. The Q redox state and oxygen consumption were measured simultaneously in isolated mitochondria. A coupling-control protocol was applied to analyze LEAK, OXPHOS, and electron transfer capacities (L, P, and E, respectively) in the succinate-pathway. In a second pathway-control protocol, NADH- and succinate-linked pathways (N and S) converge at the Q-junction. mtCoQ was more oxidized when O2 flux was stimulated in coupling-control states with load increasing from L to P and E. In contrast, mtCoQ was more reduced when O2 flux was stimulated with electron input capacities increasing from N-, S- to NS-pathway-control states. N- and S- pathway capacities were not completely additive, thus confirming partial pool behavior of Q as proposed in the plasticity model of supercomplex organization. • Keywords: Q-junction, mitochondria, oxygen consumption, Q redox state, three-electrode system, cyclic voltammetry, harmonized SUIT protocols, high-resolution respirometry, coupling control, pathway control, NS-pathway, additivity
• O2k-Network Lab: AT Innsbruck Oroboros
ORCID: 
Komlodi Timea, Cardoso Luiza HD, Doerrier Carolina, Gnaiger Erich
