Robb 2018 J Biol Chem: Difference between revisions
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{{Publication | {{Publication | ||
|title=Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP (2018) Control of mitochondrial superoxide production by reverse electron transport at complex I. J Biol Chem 293:9869-79. | |title=Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP (2018) Control of mitochondrial superoxide production by reverse electron transport at complex I. J Biol Chem 293:9869-79. https://doi.org/10.1074/jbc.RA118.003647 | ||
|info=[https://www.ncbi.nlm.nih.gov/pubmed/29743240 PMID: 29743240 Open Access] | |info=[https://www.ncbi.nlm.nih.gov/pubmed/29743240 PMID: 29743240 Open Access] | ||
|authors=Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP | |authors=Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP | ||
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|keywords=RET, Coenzyme Q, Complex I, Mitochondria, Mitochondrial membrane potential, Reactive oxygen species (ROS), Redox signaling, Respiration, Reverse electron transport, Superoxide | |keywords=RET, Coenzyme Q, Complex I, Mitochondria, Mitochondrial membrane potential, Reactive oxygen species (ROS), Redox signaling, Respiration, Reverse electron transport, Superoxide | ||
|editor=[[Kandolf G]] | |editor=[[Kandolf G]] | ||
|mipnetlab=FI Helsinki Jacobs HT, IT Padova Viscomi C | |mipnetlab=FI Helsinki Jacobs HT, IT Padova Viscomi C, DE Jena Szibor M | ||
}} | }} | ||
== Cited by == | |||
{{Template:Cited by Komlodi 2021 MitoFit AmR-O2}} | |||
{{Template:Cited by Komlodi 2021 MitoFit AmR}} | |||
{{Template:Cited by Komlodi 2021 MitoFit Tissue normoxia}} | |||
{{Template:Cited by Komlodi 2022 MitoFit ROS review}} | |||
{{Labeling | {{Labeling | ||
|area=Respiration, nDNA;cell genetics | |area=Respiration, nDNA;cell genetics | ||
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|pathways=N, S, ROX | |pathways=N, S, ROX | ||
|instruments=Oxygraph-2k, O2k-Fluorometer | |instruments=Oxygraph-2k, O2k-Fluorometer | ||
|additional=2018-07, AmR, | |additional=2018-07, AmR, MitoFit 2021 AmR, MitoFit 2021 Tissue normoxia, MitoFit 2021 AmR-O2, MitoFit 2022 ROS review | ||
}} | }} |
Latest revision as of 12:16, 22 March 2023
Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP (2018) Control of mitochondrial superoxide production by reverse electron transport at complex I. J Biol Chem 293:9869-79. https://doi.org/10.1074/jbc.RA118.003647 |
Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP (2018) J Biol Chem
Abstract: The generation of mitochondrial superoxide (O2ฬโข-)) by reverse electron transport (RET) at complex I causes oxidative damage in pathologies such as ischemia reperfusion injury, but also provides the precursor to H2O2 production in physiological mitochondrial redox signaling. Here, we quantified the factors that determine mitochondrial O2ฬโข- production by RET in isolated heart mitochondria. Measuring mitochondrial H2O2 production at a range of proton-motive force (ฮp) values and for several coenzyme Q (CoQ) and NADH pool redox states obtained with the uncoupler p-trifluoromethoxyphenylhydrazone, we show that O2ฬโข- production by RET responds to changes in O2ฬโข- concentration, the magnitude of ฮp, and the redox states of the CoQ and NADH pools. Moreover, we determined how expressing the alternative oxidase from the tunicate Ciona intestinalis to oxidize the CoQ pool affected RET-mediated O2ฬโข- production at complex I, underscoring the importance of the CoQ pool for mitochondrial O2ฬโข- production by RET. An analysis of O2ฬโข- production at complex I as a function of the thermodynamic forces driving RET at complex I revealed that many molecules that affect mitochondrial reactive oxygen species production do so by altering the overall thermodynamic driving forces of RET, rather than by directly acting on complex I. These findings clarify the factors controlling RET-mediated mitochondrial O2ฬโข- production in both pathological and physiological conditions. We conclude that O2ฬโข- production by RET is highly responsive to small changes in ฮp and the CoQ redox state, indicating that complex I RET represents a major mode of mitochondrial redox signaling. โข Keywords: RET, Coenzyme Q, Complex I, Mitochondria, Mitochondrial membrane potential, Reactive oxygen species (ROS), Redox signaling, Respiration, Reverse electron transport, Superoxide โข Bioblast editor: Kandolf G โข O2k-Network Lab: FI Helsinki Jacobs HT, IT Padova Viscomi C, DE Jena Szibor M
Cited by
- Komlรณdi T, Sobotka O, Gnaiger E (2021) Facts and artefacts on the oxygen dependence of hydrogen peroxide production using Amplex UltraRed. Bioenerg Commun 2021.4. https://doi:10.26124/BEC:2021-0004
- Komlรณdi 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).
- 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)
- Komlรณdi T, Gnaiger E (2022) Discrepancy on oxygen dependence of mitochondrial ROS production - review. MitoFit Preprints 2022 (in prep).
Labels: MiParea: Respiration, nDNA;cell genetics
Stress:Oxidative stress;RONS Organism: Rat Tissue;cell: Heart Preparation: Isolated mitochondria
Coupling state: ET
Pathway: N, S, ROX
HRR: Oxygraph-2k, O2k-Fluorometer
2018-07, AmR, MitoFit 2021 AmR, MitoFit 2021 Tissue normoxia, MitoFit 2021 AmR-O2, MitoFit 2022 ROS review