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Banerjee 2022 FEBS J

From Bioblast
Publications in the MiPMap
Banerjee R, Purhonen J, Kallijärvi J (2022) The mitochondrial coenzyme Q junction and Complex III: biochemistry and pathophysiology. FEBS J 289:6936-58.

» PMID: 34428349 Open Access

Banerjee R, Purhonen J, Kallijaervi J (2022) FEBS J

Abstract: Coenzyme Q (CoQ, ubiquinone) is the electron-carrying lipid in the mitochondrial electron transport system (ETS). In mammals, it serves as the electron acceptor for nine mitochondrial inner membrane dehydrogenases. These include the NADH dehydrogenase (Complex I, CI) and succinate dehydrogenase (Complex II, CII) but also several others that are often omitted in the context of respiratory enzymes: dihydroorotate dehydrogenase, choline dehydrogenase, electron-transferring flavoprotein dehydrogenase, mitochondrial glycerol-3-phosphate dehydrogenase, proline dehydrogenases 1 and 2, and sulfide:quinone oxidoreductase. The metabolic pathways these enzymes are involved in range from amino acid and fatty acid oxidation to nucleotide biosynthesis, methylation, and hydrogen sulfide detoxification, among many others. The CoQ-linked metabolism depends on CoQ reoxidation by the mitochondrial Complex III (cytochrome bc1 Complex, CIII). However, the literature is surprisingly limited as for the role of the CoQ-linked metabolism in the pathogenesis of human diseases of oxidative phosphorylation (OXPHOS), in which the CoQ homeostasis is directly or indirectly affected. In this review, we give an introduction to CIII function, and an overview of the pathological consequences of CIII dysfunction in humans and mice and of the CoQ-dependent metabolic processes potentially affected in these pathological states. Finally, we discuss some experimental tools to dissect the various aspects of compromised CoQ oxidation.

Bioblast editor: Gnaiger E


Enzyme: Complex II;succinate dehydrogenase, Complex III 

Pathway: NS