ArticleMolecular microbiology2014
The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025Article
- CCProtein science : a publication of the Protein Society · 2023Article
- The mitochondrial permeability transition: Recent progress and open questions.The FEBS journal · 2022Review
- Top-Down Identification and Sequence Analysis of Small Membrane Proteins Using MALDI-MS/MS.Journal of the American Society for Mass Spectrometry · 2022Article
- ATP synthase FCellular and molecular life sciences : CMLS · 2022Review
- Mitochondrial energetics with transmembrane electrostatically localized protons: do we have a thermotrophic feature?Scientific reports · 2021Article
- ATP synthase: Evolution, energetics, and membrane interactions.The Journal of general physiology · 2020Review
- Isothermal Environmental Heat Energy Utilization by Transmembrane Electrostatically Localized Protons at the Liquid-Membrane Interface.ACS omega · 2020Article
- Correlation between the numbers of rotation steps in the ATPase and proton-conducting domains of F- and V-ATPases.Biophysical reviews · 2020Article
- Unusual features of the c-ring of FScientific reports · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Convergent evolution of unusual complex I homologs with increased proton pumping capacity: energetic and ecological implications.The ISME journal · 2018Article
- Proton Dynamics at the Membrane Surface.Biophysical journal · 2016Article
- Sustainable biorefining in wastewater by engineered extreme alkaliphile Bacillus marmarensis.Scientific reports · 2016Article
- Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans.Open biology · 2015Article
- Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline.Science advances · 2015Article
- Alkaliphilic Bacteria with Impact on Industrial Applications, Concepts of Early Life Forms, and Bioenergetics of ATP Synthesis.Frontiers in bioengineering and biotechnology · 2015Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 Å resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E(54) ) on environmental hydrophobicity. Faster labelling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E(54) in the mutant due to reduced water occupancy within the H(+) binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E(54) carboxylate. The study directly connects subtle structural adaptations of the c-ring ion binding site to in vivo effects of alkaliphile cell physiology.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.