Crucial aminoacids in the FO sector of the F1 FO -ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions

Amino Acids
Fabiana TrombettiSalvatore Nesci

Abstract

The eukaryotic F1FO-ATP synthase/hydrolase activity is coupled to H+ translocation through the inner mitochondrial membrane. According to a recent model, two asymmetric H+ half-channels in the a subunit translate a transmembrane vertical H+ flux into the rotor rotation required for ATP synthesis/hydrolysis. Along the H+ pathway, conserved aminoacid residues, mainly glutamate, address H+ both in the downhill and uphill transmembrane movements to synthesize or hydrolyze ATP, respectively. Point mutations responsible for these aminoacid changes affect H+ transfer through the membrane and, as a cascade, result in mitochondrial dysfunctions and related pathologies. The involvement of specific aminoacid residues in driving H+ along their transmembrane pathway within a subunit, sustained by the literature and calculated data, leads to depict a model consistent with some mitochondrial disorders.

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Citations

Jul 4, 2019·SLAS Discovery·Salvatore NesciAlessandra Pagliarani
Dec 31, 2020·Proteins·Salvatore Nesci, Alessandra Pagliarani
Jul 23, 2019·Archives of Biochemistry and Biophysics·Samah RaheemZulfiqar Ahmad

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