Journal
JOURNAL OF INHERITED METABOLIC DISEASE
Volume 35, Issue 2, Pages 211-225Publisher
WILEY
DOI: 10.1007/s10545-011-9382-9
Keywords
-
Funding
- Prinses Beatrix Fonds [OP-05-04]
Ask authors/readers for more resources
Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F-1, situated in the mitochondrial matrix, and F-o, 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available