Voltage-gated proton channels and other proton transfer pathways
TE Decoursey - Physiological reviews, 2003 - journals.physiology.org
Proton channels exist in a wide variety of membrane proteins where they transport protons
rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules …
rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules …
Rotation and structure of FoF1-ATP synthase
Abstract F o F 1-ATP synthase is one of the most ubiquitous enzymes; it is found widely in
the biological world, including the plasma membrane of bacteria, inner membrane of …
the biological world, including the plasma membrane of bacteria, inner membrane of …
Artificial photosynthetic cell producing energy for protein synthesis
Attempts to construct an artificial cell have widened our understanding of living organisms.
Many intracellular systems have been reconstructed by assembling molecules, however the …
Many intracellular systems have been reconstructed by assembling molecules, however the …
Structure of a bacterial ATP synthase
ATP synthases produce ATP from ADP and inorganic phosphate with energy from a
transmembrane proton motive force. Bacterial ATP synthases have been studied extensively …
transmembrane proton motive force. Bacterial ATP synthases have been studied extensively …
Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase
A Nakano, J Kishikawa, K Mitsuoka… - Nature …, 2023 - nature.com
F1 domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit
proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP …
proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP …
Conserved in situ arrangement of complex I and III2 in mitochondrial respiratory chain supercomplexes of mammals, yeast, and plants
KM Davies, TB Blum… - Proceedings of the …, 2018 - National Acad Sciences
We used electron cryo-tomography and subtomogram averaging to investigate the structure
of complex I and its supramolecular assemblies in the inner mitochondrial membrane of …
of complex I and its supramolecular assemblies in the inner mitochondrial membrane of …
Escherichia coli phage‐shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes
R Kobayashi, T Suzuki, M Yoshida - Molecular microbiology, 2007 - Wiley Online Library
Escherichia coli phage‐shock protein A (PspA), a 25.3 kDa peripheral membrane protein, is
induced under the membrane stress conditions and is assumed to help maintain membrane …
induced under the membrane stress conditions and is assumed to help maintain membrane …
F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ϵ subunit in response to proton motive force and ADP/ATP balance
The ϵ subunit in F 0 F 1-ATPase/synthase undergoes drastic conformational rearrangement,
which involves the transition of two C-terminal helices between a hairpin" down"-state and …
which involves the transition of two C-terminal helices between a hairpin" down"-state and …
A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles
S Schenck, SM Wojcik, N Brose, S Takamori - Nature neuroscience, 2009 - nature.com
Uptake of glutamate into synaptic vesicles is mediated by vesicular glutamate transporters
(VGLUTs). Although glutamate uptake has been shown to depend critically on Cl−, the …
(VGLUTs). Although glutamate uptake has been shown to depend critically on Cl−, the …
ATP-driven stepwise rotation of FoF1-ATP synthase
H Ueno, T Suzuki, K Kinosita Jr… - Proceedings of the …, 2005 - National Acad Sciences
FoF1-ATP synthase (FoF1) is a motor enzyme that couples ATP synthesis/hydrolysis with a
transmembrane proton translocation. F1, a water-soluble ATPase portion of FoF1, rotates by …
transmembrane proton translocation. F1, a water-soluble ATPase portion of FoF1, rotates by …