Cookies help us deliver our services. By using our services, you agree to our use of cookies. More information

Jarmuszkiewicz 2023 Front Biosci (Landmark Ed)

From Bioblast
Publications in the MiPMap
Jarmuszkiewicz W, Dominiak K, Budzinska A, Wojcicki K, Galganski L (2023) Mitochondrial coenzyme Q redox homeostasis and reactive oxygen species production. https://doi.org/10.31083/j.fbl2803061

» Front Biosci (Landmark Ed) 28:61. Open Access

Jarmuszkiewicz Wieslawa, Dominiak Karolina, Budzinska Adrianna, Wojcicki Krzysztof, Galganski Lukasz (2023) Front Biosci (Landmark Ed)

Abstract: Mitochondrial coenzyme Q (mtQ) of the inner mitochondrial membrane is a redox active mobile carrier in the respiratory chain that transfers electrons between reducing dehydrogenases and oxidizing pathway(s). mtQ is also involved in mitochondrial reactive oxygen species (mtROS) formation through the mitochondrial respiratory chain. Some mtQ-binding sites related to the respiratory chain can directly form the superoxide anion from semiubiquinone radicals. On the other hand, reduced mtQ (ubiquinol, mtQH2) recycles other antioxidants and directly acts on free radicals, preventing oxidative modifications. The redox state of the mtQ pool is a central bioenergetic patameter that alters in response to changes in mitochondrial function. It reflects mitochondrial bioenergetic activity and mtROS formation level, and thus the oxidative stress associated with the mitochondria. Surprisingly, there are few studies describing a direct relationship between the mtQ redox state and mtROS production under physiological and pathological conditions. Here, we provide a first overview of what is known about the factors affecting mtQ redox homeostasis and its relationship to mtROS production. We have proposed that the level of reduction (the endogenous redox state) of mtQ may be a useful indirect marker to assess total mtROS formation. A higher mtQ reduction level (mtQH2/mtQtotal) indicates greater mtROS formation. The mtQ reduction level, and thus the mtROS formation, depends on the size of the mtQ pool and the activity of the mtQ-reducing and mtQH2-oxidizing pathway(s) of respiratory chain. We focus on a number of physiological and pathophysiological factors affecting the amount of mtQ and thus its redox homeostasis and mtROS production level.

Bioblast editor: Gnaiger E

Selected quote

  • "Presumably, the recent advancement in the technique of simultaneous kinetic measurement of oxygen consumption and mtQ redox state by combining a Clark-type oxygen electrode and a Q-type electrode [28,129] will contribute to the widespread measurement of the redox state of mtQ in isolated respiring mitochondria."
28. 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. https://doi.org/10.26124/bec:2021-0003
Jarmuszkiewicz 2023 Front Biosci CORRECTION.png

Correction: FADH2 and Complex II

Ambiguity alert.png
FADH2 is shown as the substrate feeding electrons into Complex II (CII). This is wrong and requires correction - for details see Gnaiger (2024).
Gnaiger E (2024) Complex II ambiguities ― FADH2 in the electron transfer system. J Biol Chem 300:105470. https://doi.org/10.1016/j.jbc.2023.105470 - »Bioblast link«

On terminology

» Mitochondrial states and rates - terminology beyond MitoEAGLE 2020
For harmonization of terminology on respiratory states and rates, see

Labels:






Outdated terminology 


Labels:

Stress:Oxidative stress;RONS 



Regulation: Redox state