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Crucial aminoacids in the FO sector of the F1FO-ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions
- Source :
- Amino Acids. 51:579-587
- Publication Year :
- 2019
- Publisher :
- Springer Science and Business Media LLC, 2019.
-
Abstract
- The eukaryotic F 1 F O -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.
- Subjects :
- 0301 basic medicine
Mitochondrial disease
Protein subunit
Clinical Biochemistry
Biochemistry
F 1 F O -ATP synthase
03 medical and health sciences
a Subunit
medicine
H + pathway
Inner mitochondrial membrane
Crucial aminoacid
030102 biochemistry & molecular biology
ATP synthase
biology
Chemistry
Point mutation
Organic Chemistry
Glutamate receptor
medicine.disease
Transmembrane protein
030104 developmental biology
biology.protein
Biophysics
Mitochondrial dysfunction
Flux (metabolism)
Subjects
Details
- ISSN :
- 14382199 and 09394451
- Volume :
- 51
- Database :
- OpenAIRE
- Journal :
- Amino Acids
- Accession number :
- edsair.doi.dedup.....1d6ba13cd01ef49b9e650f4d0dd1818f