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Tabassum 2020 J Biomed Res Environ Sci

From Bioblast
Publications in the MiPMap
Tabassum N, Kheya IS, Ibn Asaduzzaman SA, Maniha SM, Fayz AH, Zakaria A, Fayz AH, Zakaria A, Noor R (2020) A review on the possible leakage of electrons through the electron transport chain within mitochondria. J Biomed Res Environ Sci 1:105-13. https://doi.org/10.37871/jels1127


Tabassum N, Kheya IS, Ibn Asaduzzaman SA, Maniha SM, Fayz AH, Zakaria A, Fayz AH, Zakaria A, Noor R (2020) J Biomed Res Environ Sci

Abstract: The finding of electron leakage during the electron transport within the mitochondrial membrane (in eukaryotes) or in the cell membrane of the prokaryotes is an important issue for the accumulation of the Reactive Oxygen Species (ROS) in the cytosol which in turn induce the probable aging of cells. In eukaryotes, mitochondrion is known to be the major site of the ROS generation in different pathological processes which may further cause cell damages as evident through the ischemia-reperfusion (I/R) injury, respiratory diseases, cell apoptosis, and even the onset of cancer. Thus, the mitochondrial leakage and the physiological effect of leaked protons and electrons grow up with future interest in energy metabolism. Current review focused on the physiological impact of electron/ proton leakage particularly in the eukaryotic cells based on the previous reports; emphasized on the prospects of the eukaryotic mitochondrion as a modulator of proton and electron leakage; and finally attempted to assess the regulatory mechanisms of such electron/ proton leakage.

Bioblast editor: Gnaiger E

Tabassum 2020 J Biomed Res Environ Sci 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«


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Enzyme: Complex II;succinate dehydrogenase