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The Thomson problem is a natural consequence of J. J. Thomson's plum pudding model in the absence of its uniform positive background charge. [ 12 ] "No fact discovered about the atom can be trivial, nor fail to accelerate the progress of physical science, for the greater part of natural philosophy is the outcome of the structure and mechanism ...
Plaque commemorating J. J. Thomson's discovery of the electron outside the old Cavendish Laboratory in Cambridge Autochrome portrait by Georges Chevalier, 1923 Thomson c. 1920–1925 Thomson was elected a Fellow of the Royal Society (FRS) [ 25 ] [ 50 ] and appointed to the Cavendish Professorship of Experimental Physics at the Cavendish ...
An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.
These electrons enter the electron transport chain of the mitochondria via reduction equivalents to generate ATP. The shuttle system is required because the mitochondrial inner membrane is impermeable to NADH, the primary reducing equivalent of the electron transport chain.
The mitochondrial shuttles are biochemical transport systems used to transport reducing agents across the inner mitochondrial membrane. NADH as well as NAD+ cannot cross the membrane, but it can reduce another molecule like FAD and [QH 2] that can cross the membrane, so that its electrons can reach the electron transport chain.
The last steps of this process occur in mitochondria. The reduced molecules NADH and FADH 2 are generated by the Krebs cycle, glycolysis, and pyruvate processing. These molecules pass electrons to an electron transport chain, which releases the energy of oxygen to create a proton gradient across the inner mitochondrial membrane.
The glycerol phosphate shuttle was first characterized as a major route of mitochondrial hydride transport in the flight muscles of blow flies. [5] [6] It was initially believed that the system would be inactive in mammals due to the predominance of lactate dehydrogenase activity over glycerol-3-phosphate dehydrogenase 1 (GPD1) [5] [7] until high GPD1 and GPD2 activity were demonstrated in ...
Mitochondrial glycerol-3-phosphate dehydrogenase (GPD2), catalyzes the irreversible oxidation of glycerol-3-phosphate to dihydroxyacetone phosphate and concomitantly transfers two electrons from FAD to the electron transport chain. GPD2 consists of 4 identical subunits. [10] GPD2 Reaction Mechanism