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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
Halalkalibacterium halodurans
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
Desulforamulus reducens
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
Alkalihalophilus pseudofirmus
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
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among eukaryotes, complex V from Chlamydomonadales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel
evolution
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among eukaryotes, complex V from Chlorococcales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel
evolution
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among eukaryotes, complex V from Sphaeropleales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel
evolution
the general structure and core subunits of the F1FO ATP synthase are highly conserved from bacteria to fungi, plants and animals
evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
Alkalihalophilus pseudofirmus OF4
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
Desulforamulus reducens MI-1
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
Halalkalibacterium halodurans C-125
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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evolution
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ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
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malfunction
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deletion of the 3'-UTR in the ATP2 gene leads to deficient protein import and reduced ATP synthesis, mtDNA depletion and respiratory dysfunction
malfunction
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down-regulation of beta-F1-ATPase expression in chronic myeloid leukemia leads to adriamycin resistance. Deletion of IEX-1, a stress-inducible gene that apparently targets IF1 for degradation, results in the inhibition of the ATP synthase activity in vivo. Relevance of mitochondrial dysfunction as a central player of tumorigenesis, mechanisms participating in controlling the content and activity of the H+-ATP synthase, which is a bottleneck component of oxidative phosphorylation, overview
malfunction
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Escherichia coli FoF1-ATP synthase atp mutant strain DK8 lacks hydrogenase activity during fermentative growth on glucose at pH 7.0, while at pH 5.5 hydrogenase activity is only 20% that of the wild-type
malfunction
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expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane. Yeast mutants lacking beta subunit have stable aggregated F1 alpha subunit in the mitochondrial matrix
malfunction
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HeLa cells lacking F1 degrade Saccharomyces cerevisiae Atp6p, thereby preventing proton leakage across the inner membrane. The human alpha subunit is completely degraded in cells deficient in F1 beta subunit. Depletion of the F1 beta subunit in the mutant shbeta-3 HeLa cell line elicits a remarkable decrease of alpha subunit. In MR6DATP1 lacking the F1 alpha subunit, the F1 beta subunit fails to assemble into the F1 oligomer and forms aggregates that resist solubilization by non-denaturing detergents such as lauryl maltoside
malfunction
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lethal phenotype of the epsilon knock-out mutant
malfunction
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loss of Asa7 atypical subunit in Chlamydomonas reinhardtii leads to an unstable complex V and increased sensitivity to oligomycin impared to the wild-type
malfunction
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lysine substitution of the alpha subunit catalytically critical Arg364 residue causes frequent pauses because of severe ADP inhibition, and a slight decrease in ATP binding rate
malfunction
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the siRNA-mediated downregulation of the beta subunit of the F1Fo-ATPase reduces influenza virion formation and virus growth in cell culture
malfunction
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virion formation/Budding of Influenza virus particles is reduced in F1beta-depleted cells
malfunction
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silencing of subunit ATPase Tb2 inhibits cell growth by decreasing the mitochondrial membrane potential in bloodstream form of Trypanosoma brucei. Depletion of subunit ATPase Tb2 does not significantly alter ATP hydrolysis capabilities but affects cell growth, the mitochondrial membrane potential and FoF1-ATPase integrity in dyskinetoplastic Trypanosoma brucei evansi
malfunction
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lysine substitution of the alpha subunit catalytically critical Arg364 residue causes frequent pauses because of severe ADP inhibition, and a slight decrease in ATP binding rate
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metabolism
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F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis. Chloroplast F1-ATPase is subject to redox regulation, whereby ATP hydrolysis activity is regulated by formation and reduction of the disulfide bond located on the gamma-subunit, molecular mechanism, overview
metabolism
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internal inhibition of ATP hydrolysis activity of F0F1-ATP synthase is very important for cyanobacteria that are exposed to prolonged dark adaptation and, in general, for the survival of photosynthetic organisms in an ever-changing environment
metabolism
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repression of the bioenergetic function of mitochondria is one of the strategies of the cancer cell in order to ensure its proliferation by diminishing the potential to execute ROS-mediated cell death
metabolism
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the coupling of conformational cycle to electrochemical gradient is an efficient means of energy transduction and regulation, for ion binding to the membrane domain, known as Fo, is appropriately selective. H+ selectivity is most likely a robust property of all Fo rotors. In H+-coupled rotors, the incorporation of hydrophobic side chains to the binding sites enhances this inherent H+ selectivity. Size restriction may also favor H+ over Na+, but increasing size alone does not confer Na+ selectivity
metabolism
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in order to synthesize ATP, the enzyme is capable of rotating its central rotor in a reversible manner. In the clockwise direction, it functions as ATP synthase, while in counter clockwise sense it functions as a proton pumping ATPase
metabolism
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the enzyme energizes the inner mitochondrial membrane by coupling ATP hydrolysis with the exchange of ADP3- for ATP4- by the ATP/ADP carrier
metabolism
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the enzyme modulates signaling pathways that activate the mitohormetic response, namely ATP, reactive oxygen species, and target of rapamycin
metabolism
the enzyme uses the proton motive force across the bacterial plasma membrane to drive rotation of the central rotor subunits within a stator subunit complex. Through this mechanical rotation, the rotor coordinates three nucleotide binding sites that sequentially catalyze the synthesis of ATP. Moreover, the enzyme can hydrolyze ATP to turn the rotor in the opposite direction and generate proton motive force
physiological function
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F1-ATPase is a rotary molecular motor in which the gamma-subunit rotates against the alpha3beta3 cylinder. The unitary gamma-rotation is a 120° step comprising 80° and 40° substeps, each of these initiated by ATP binding and ADP release and by ATP hydrolysis and inorganic phosphate release, respectively
physiological function
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F1Fo-ATP synthase is a key enzyme of oxidative phosphorylation that is localized in the inner membrane of mitochondria. It uses the energy stored in the proton gradient across the inner mitochondrial membrane to catalyze the synthesis of ATP from ADP and phosphate
physiological function
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FoF1-ATP synthase is an enzyme that is responsible for ATP synthesis during oxidative phosphorylation and photosynthesis. FoF1 is a complex of two rotary motors F1 and Fo, and the ATP synthesis/hydrolysis reaction that is reversibly catalyzed by F1 is coupled with proton transport across membrane-embedded Fo
physiological function
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FOF1-ATP synthase synthesizes cellular ATP from ADP and inorganic phosphate. The FOF1-ATP synthase is localized in the mitochondria of eukaryotic cells, where it utilizes the electrochemical gradient, established across the inner mitochondrial membrane by oxidative phosphorylation, for the synthesis of ATP from ADP and inorganic phosphate. Recombinant ATP synthase alpha suppresses huntingtin aggregation when transiently overexpressed in SH-SY5Y cells, overview
physiological function
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FoF1-ATPase/synthase consists of two rotary molecular motors: a water-soluble, ATP-driven F1 motor and a membrane embedded, H+-driven Fo motor. These molecular motors are connected together to couple ATP synthesis/hydrolysis and ion flow.The F1-ATPase hydrolyzes ATP into ADP and inorganic phosphate, and the hydrolysis of one ATP drives discrete 120° rotation of the gammaepsilon subunits relative to the other subunits
physiological function
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role of the F1Fo ATP synthase in iron transport, and involvement of proton-coupled transport associated with the cgamma subunit
physiological function
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the aurovertin B-sensitive ATPase activity of ecto-FOF1 is markedly inhibited in cholestatic rats, to about 45% of that from control rats
physiological function
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the enzyme is an essential machine of the power stations of the cell. In principle, it can operate in either direction, to synthesize ATP at the expense of ion flow, or to drive ion flow while hydrolysing ATP, although this sometimes occurs only in the forward direction
physiological function
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the enzyme is an essential machine of the power stations of the cell. In principle, it can operate in either direction, to synthesize ATP at the expense of ion flow, or to drive ion flow while hydrolysing ATP, although this sometimes occurs only in the forward direction
physiological function
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the protons secreted by the enzyme in osteoclast membrane into the closed extracellular compartment are essential for demineralization of calcified bone
physiological function
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v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells
physiological function
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efficient influenza virion formation requires the ATPase activity of F1Fo-ATPase. Plasma membrane-associated, but not mitochondrial, F1Fo-ATPase, is important for influenza virion formation and budding, and release from cells
physiological function
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F1-ATPase is an ATP-driven rotary motor protein in which the gamma-subunit rotates against the catalytic stator ring
physiological function
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FoF1-ATP synthase is the main membrane protein complex of bioenergetic relevance catalyzing ATP synthesis as terminal step in oxidative phosphorylation. Requirement for the FoF1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases Hyd-1 and Hyd-2
physiological function
Na+-dependent F1F0-ATP synthase in the cytoplasmic membrane plays a potential role in salt-stress tolerance
physiological function
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the functional mechanism of the F1Fo ATP synthase entails a conformational cycle that is coupled to the movement of H+ or Na+ ions across its transmembrane domain, down an electrochemical gradient
physiological function
the hydrophilic F1 component catalyzes ATP formation and protrudes into the matrix, while the hydrophobic FO component channels protons through the membrane and anchors the entire complex to the mitochondrial inner membrane
physiological function
ATP synthase subunit a deletion results in an increased motility phenotype. The amount of membrane-bound ATPase is reduced in the mutants. Deletion or mutation confers faster motility in low concentrations of sodium than in the parental strain and this phenotype is suppressed in the presence of KCN
physiological function
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F1-ATPase serves as a receptor for a gastrointestinal peptide mediating cell growth
physiological function
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at the plant vacuole enzyme, the is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
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overexpression of subunit VHA-A confers transgenic tobacco seedlings with enhanced vacuole H+-ATPase activity and improved drought tolerance
physiological function
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the enzyme can support general mitochondrial and cellular functions, working in extremely efficient energy saving reverse mode and flexibly recruiting free radical detoxication and ATP producing / transporting pathways
physiological function
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the membrane-bound ATPaseTb2 subunit is essential for maintaining normal growth and the mitochondrial membrane potential of dyskinetoplastic cells
physiological function
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the robust ATP-hydrolyzing activity occurs in ischemia for maintaining the transmembrane proton motive force of mitochondria inner membrane
physiological function
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F1-ATPase is an ATP-driven rotary motor protein in which the gamma-subunit rotates against the catalytic stator ring
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additional information
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Ca2+ facilitates a dynamin- and V-ATPase-dependent endocytosis in association with with an inhibition of the plasma membrane V-ATPase, overview
additional information
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FOF1-ATP synthase plays a role in neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease
additional information
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pigment epithelium-derived factor-mediated inhibition of ATP synthase may form part of the biochemical mechanisms by which PEDF exerts its antiangiogenic activity
additional information
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pigment epithelium-derived factor-mediated inhibition of ATP synthase may form part of the biochemical mechanisms by which PEDF exerts its antiangiogenic activity
additional information
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the atpD mutant strain MS116 expresses the FoF1 ATPase to the level as wild-type one, but it has significantly lowered H+ efflux and ATPase activity, overview
additional information
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Asn90 is located in the middle of putative second transmembrane helix and likely to play an important role in H+-translocation
additional information
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ATP2 mRNA is no Puf3p target and belongs to the class of Puf3-independent mitochondria-localized mRNAs
additional information
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expression of the catalytic subunit beta-F1-ATPase is tightly regulated at post-transcriptional levels during mammalian development and in the cell cycle. Downregulation of beta-F1-ATPase is a hallmark of most human carcinomas. Role of the ATPase inhibitor factor 1 and of Ras-GAP SH3 binding protein 1, G3BP1, controlling the activity of the H+-ATP synthase and the translation of beta-F1-ATPase mRNA respectively in cancer cells
additional information
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expression of the catalytic subunit beta-F1-ATPase is tightly regulated at post-transcriptional levels during mammalian development and in the cell cycle. Downregulation of beta-F1-ATPase is a hallmark of most human carcinomas. Role of the ATPase inhibitor factor 1 and of Ras-GAP SH3 binding protein 1, G3BP1, controlling the activity of the H+-ATP synthase and the translation of beta-F1-ATPase mRNA respectively in cancer cells. A trans-acting factor that regulate beta-F1-ATPasemRNA translation, is G3BP1, Ras-GAP SH3 binding protein 1, that interacts with the 3'UTR of beta-mRNA, the interaction specifically represses mRNA translation by preventing its recruitment into active polysomes
additional information
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F1-ATPase is a water-soluble portion of the FoF1-ATP synthase and an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine at position 364, termed the arginine finger, with stereogeometric similarities with the arginine finger of G-protein-activating proteins. The principal role of the arginine finger is not to mediate cooperativity among the catalytic sites, but to enhance the rate of the ATP cleavage by stabilizing the transition state of ATP hydrolysis
additional information
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F1-ATPase is the isolated extrinsic part of ATP synthase, the extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
additional information
modular assembly of the F1Fo ATP synthase. F1 precursor proteins are imported and rapidly assembled into both apparently free F1 and F1FO ATP synthase in organello
additional information
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molecular dynamics simulations and free-energy calculations of ion coordination and transfer in wild-type enzyme and mutant A63S, overview
additional information
NP_393483
the peripheral stalk of the A1A0-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. The BNT peptide specifically interacts with 26 residues of the ECT1HCT domain
additional information
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the peripheral stalk of the A1A0-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. The BNT peptide specifically interacts with 26 residues of the ECT1HCT domain
additional information
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F1-ATPase is a water-soluble portion of the FoF1-ATP synthase and an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine at position 364, termed the arginine finger, with stereogeometric similarities with the arginine finger of G-protein-activating proteins. The principal role of the arginine finger is not to mediate cooperativity among the catalytic sites, but to enhance the rate of the ATP cleavage by stabilizing the transition state of ATP hydrolysis
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additional information
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Asn90 is located in the middle of putative second transmembrane helix and likely to play an important role in H+-translocation
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additional information
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the atpD mutant strain MS116 expresses the FoF1 ATPase to the level as wild-type one, but it has significantly lowered H+ efflux and ATPase activity, overview
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