Klusch 2017 Elife

From Bioblast
Jump to: navigation, search
Publications in the MiPMap
Klusch N, Murphy BJ, Mills DJ, Yildiz Ö, Kühlbrandt W (2017) Structural basis of proton translocation and force generation in mitochondrial ATP synthase. Elife e33274. doi: 10.7554/eLife.33274.

» PMID: 29210357 Open Access

Klusch N, Murphy BJ, Mills DJ, Yildiz O, Kuehlbrandt W (2017) Elife

Abstract: ATP synthases produce ATP by rotary catalysis, powered by the electrochemical proton gradient across the membrane. Understanding this fundamental process requires an atomic model of the proton pathway. We determined the structure of an intact mitochondrial ATP synthase dimer by electron cryo-microscopy at near-atomic resolution. Charged and polar residues of the a-subunit stator define two aqueous channels, each spanning one half of the membrane. Passing through a conserved membrane-intrinsic helix hairpin, the lumenal channel protonates an acidic glutamate in the c-ring rotor. Upon ring rotation, the protonated glutamate encounters the matrix channel and deprotonates. An arginine between the two channels prevents proton leakage. The steep potential gradient over the sub-nm inter-channel distance exerts a force on the deprotonated glutamate, resulting in net directional rotation.

Keywords: ATP synthase; biochemistry; biophysics; electron cryo-microscopy; energy conversion; membrane potential; membrane protein structure; mitochondria; structural biology Bioblast editor: Gnaiger E

Cited by

Gnaiger 2020 BEC MitoPathways


Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5th ed. Bioenerg Commun 2020.2:112 pp. doi:10.26124/bec:2020-0002


Labels:



Enzyme: Complex V;ATP synthase  Regulation: Coupling efficiency;uncoupling, mt-Membrane potential 



BEC 2020.2