Mitochondrial ATP synthase: architecture, function and pathology

By A. Jonckheere, J. Smeitink, R. Rodenburg. Journal of Inherited Metabolic Disease, 2011

600 citations recorded by the source corpus.

Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F1, situated in the mitochondrial matrix, and Fo, located in the inner mitochondrial membrane. Complex V uses the energy created by the proton electrochemical gradient to phosphorylate ADP to ATP. This review covers the architecture, function and assembly of complex V. The role of complex V di-and oligomerization and its relation with mitochondrial morphology is discussed. Finally, pathology related to complex V deficiency and current therapeutic strategies are highlighted. Despite the huge progress in this research field over the past decades, questions remain to be answered regarding the structure of subunits, the function of the rotary nanomotor at a molecular level, and the human complex V assembly process. The elucidation of more nuclear genetic defects will guide physio(patho)logical studies, paving the way for future therapeutic interventions.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0b8bbdfed6f6256036489597d4b168f995a16f73

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Citations in the corpus

• Mitochondrial electron transport chain, ROS generation and uncoupling (Review) (2019, background): “Then, the protons pass from the IMS to the matrix through F 0 , which transfers the stored energy created by the proton electrochemical gradient to F 1 , causing a conformational change in F 1 F 0 ATP synthase so that AdP can be phosphorylated to form ATP (41).”