Difference between revisions of "Cardoso 2022 Abstract Bioblast"
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|info=[https://wiki.oroboros.at/index.php/Bioblast_2022#Submitted_abstracts Bioblast 2022: BEC Inaugural Conference] | |info=[https://wiki.oroboros.at/index.php/Bioblast_2022#Submitted_abstracts Bioblast 2022: BEC Inaugural Conference] | ||
|authors=Oroboros | |authors=Oroboros | ||
|abstract=NADH-linked substrates (N-substrates) of TCA-cycle and other mt-matrix dehydrogenases feed electrons through the N-junction into Complex I. The redox states of the NAD-pool — defined as the sum of NAD(P)<sup>+</sup> and NAD(P)H — and of the electron transfer (ET)-reactive coenzyme Q-pool are linked in the N-pathway but are regulated independently by several convergent electron entries into the Q-junction [1]. Complementary to ET-pathway control of respiratory rate and redox state (redox push by electron input), coupling control exerts opposite effects on the metabolic parameters. Whereas redox push reduces the N- and Q-pool in the LEAK state at low O<sub>2</sub> flux and high protonomotive force ''pmF'', stimulation of O<sub>2</sub> flux by ADP in the OXPHOS state [2] is accompanied by a redox pull to the oxidized state. Under these conditions, ET-pathways converging at the Q-junction yield partial additivity of O<sub>2</sub> flux, when ET-capacity downstream of Q and phosphorylation capacity exert flux control [1]. Monitoring of respiration together with NAD(P)H autofluorescence and Q-redox state [3] provides unique analytical and diagnostic power in the study of mitochondrial respiratory control at the Q-junction. | |abstract=NADH-linked substrates (N-substrates) of TCA-cycle and other mt-matrix dehydrogenases feed electrons through the N-junction into Complex I. The redox states of the NAD-pool — defined as the sum of NAD(P)<sup>+</sup> and NAD(P)H — and of the electron transfer (ET)-reactive coenzyme Q-pool are linked in the N-pathway but are regulated independently by several convergent electron entries into the Q-junction [1]. Complementary to ET-pathway control of respiratory rate and redox state (redox push by electron input), coupling control exerts opposite effects on the metabolic parameters. Whereas redox push reduces the N- and Q-pool in the LEAK state at low O<sub>2</sub> flux and high protonomotive force ''pmF'', stimulation of O<sub>2</sub> flux by ADP in the OXPHOS state [2] is accompanied by a redox pull to the oxidized state. Under these conditions, ET-pathways converging at the Q-junction yield partial additivity of O<sub>2</sub> flux, when ET-capacity downstream of Q and phosphorylation capacity exert flux control [1]. Monitoring of respiration together with NAD(P)H autofluorescence and Q-redox state [3] provides unique analytical and diagnostic power in the study of mitochondrial respiratory control at the Q-junction. | ||
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# Gnaiger E et al ― MitoEAGLE Task Group (2020) Mitochondrial physiology. Bioenerg Commun 2020.1. https://doi.org/10.26124/bec:2020-0001.v1 | # Gnaiger E et al ― MitoEAGLE Task Group (2020) Mitochondrial physiology. Bioenerg Commun 2020.1. https://doi.org/10.26124/bec:2020-0001.v1 | ||
# 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 | # 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 | ||
|mipnetlab=AT Innsbruck Oroboros | |mipnetlab=AT Innsbruck Oroboros | ||
|articletype=Abstract | |||
}} | |||
{{Labeling | |||
|area=Respiration | |||
|organism=Mouse | |||
|tissues=Liver, HEK | |||
|preparations=Permeabilized cells, Isolated mitochondria | |||
|couplingstates=LEAK, OXPHOS, ET | |||
|pathways=N, S, NS, ROX | |||
|instruments=Oxygraph-2k, NextGen-O2k | |||
|articletype=Abstract | |articletype=Abstract | ||
}} | }} | ||
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== Help == | == Help == | ||
* [[MitoPedia: Terms and abbreviations]] | * [[MitoPedia: Terms and abbreviations]] | ||
Revision as of 10:10, 14 May 2022
| Cardoso LHD, Gnaiger E (2022) Redox monitoring and respiration - a new horizon with the NextGen-O2k. Bioblast 2022: BEC Inaugural Conference. |
Link: Bioblast 2022: BEC Inaugural Conference
Oroboros ()
Event:
NADH-linked substrates (N-substrates) of TCA-cycle and other mt-matrix dehydrogenases feed electrons through the N-junction into Complex I. The redox states of the NAD-pool — defined as the sum of NAD(P)+ and NAD(P)H — and of the electron transfer (ET)-reactive coenzyme Q-pool are linked in the N-pathway but are regulated independently by several convergent electron entries into the Q-junction [1]. Complementary to ET-pathway control of respiratory rate and redox state (redox push by electron input), coupling control exerts opposite effects on the metabolic parameters. Whereas redox push reduces the N- and Q-pool in the LEAK state at low O2 flux and high protonomotive force pmF, stimulation of O2 flux by ADP in the OXPHOS state [2] is accompanied by a redox pull to the oxidized state. Under these conditions, ET-pathways converging at the Q-junction yield partial additivity of O2 flux, when ET-capacity downstream of Q and phosphorylation capacity exert flux control [1]. Monitoring of respiration together with NAD(P)H autofluorescence and Q-redox state [3] provides unique analytical and diagnostic power in the study of mitochondrial respiratory control at the Q-junction.
- Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5th ed. Bioenerg Commun 2020.2. https://doi.org/10.26124/bec:2020-0002
- Gnaiger E et al ― MitoEAGLE Task Group (2020) Mitochondrial physiology. Bioenerg Commun 2020.1. https://doi.org/10.26124/bec:2020-0001.v1
- 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
• O2k-Network Lab: AT Innsbruck Oroboros
Labels: MiParea: Respiration
Organism: Mouse
Tissue;cell: Liver, HEK
Preparation: Permeabilized cells, Isolated mitochondria
Coupling state: LEAK, OXPHOS, ET
Pathway: N, S, NS, ROX
HRR: Oxygraph-2k, NextGen-O2k
Affiliations and support
- Oroboros Instruments GmbH, Innsbruck, Austria
- This work was part of the Oroboros NextGen-O2k project, with funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement nº 859770.
