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Chinopoulos 2019 Int J Biochem Cell Biol

From Bioblast
Publications in the MiPMap
Chinopoulos C (2019) Succinate in ischemia: Where does it come from? Int J Biochem Cell Biol 115:105580.

ยป PMID: 31394174

Chinopoulos C (2019) Int J Biochem Cell Biol

Abstract: During tissue ischemia succinate accumulates. Herein, literature spanning the past nine decades is reviewed leaning towards the far greater role of Krebs cycle's canonical activity yielding succinate through ฮฑ-ketoglutarate -> succinyl-CoA -> succinate even in hypoxia, as opposed to reversal of succinate dehydrogenase. Furthermore, the concepts of i) a diode-like property of succinate dehydrogenase rendering it difficult to reverse, and ii) the absence of mammalian mitochondrial quinones exhibiting redox potentials in the [-60, -80] mV range needed for fumarate reduction, are discussed. Finally, it is emphasized that a "fumarate reductase" enzyme entity reducing fumarate to succinate found in some bacteria and lower eukaryotes remains to be discovered in mammalian mitochondria.

โ€ข Bioblast editor: Gnaiger E

Selected quotations

  • "The reaction catalyzed by SDH exhibits a ฮ”G of -0.59 kj/mol (Chinopoulos, 2013), thus, from the thermodynamic point of view it is reversible. Indeed, SDH reversibility was shown by Thunberg in 1925 (Thunberg, 1925); this was re-addressed by Massey and Singer in 1957 (Massey and Singer, 1957a). More specifically, they used specific electron carriers in order to demonstrate reversibility of isolated SDH (Massey and Singer, 1957b). Likewise, by using such carriers, the group of Cecchini showed that the reaction catalyzed by mammalian SDH in reverse is ~40 times slower than that in forward mode (Maklashina et al., 2018)."