ArticleThe Journal of biological chemistry2013
Membrane Na+-pyrophosphatases can transport protons at low sodium concentrations.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- NaInternational journal of molecular sciences · 2024Article
- HParasitology research · 2024Review
- Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases.EMBO reports · 2024Article
- Review
- Pre-steady-state kinetics and solvent isotope effects support the "billiard-type" transport mechanism in NaProtein science : a publication of the Protein Society · 2022Article
- The Mechanism of Energy Coupling in HInternational journal of molecular sciences · 2022Review
- Energy Coupling in Cation-Pumping Pyrophosphatase-Back to Mitchell.Frontiers in plant science · 2020Article
- The Function of Membrane Integral Pyrophosphatases From Whole Organism to Single Molecule.Frontiers in molecular biosciences · 2019Review
- Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism.Nature communications · 2016Article
- Insights into the structure and function of HV1 from a meta-analysis of mutation studies.The Journal of general physiology · 2016Review
- Real-time kinetics of electrogenic Na(+) transport by rhodopsin from the marine flavobacterium Dokdonia sp. PRO95.Scientific reports · 2016Article
- The Voltage-Gated Proton Channel: A Riddle, Wrapped in a Mystery, inside an Enigma.Biochemistry · 2015Review
- Selectivity Mechanism of the Voltage-gated Proton Channel, HV1.Scientific reports · 2015Article
- On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Minimization of extracellular space as a driving force in prokaryote association and the origin of eukaryotes.Biology direct · 2014Article
- On an early gene for membrane-integral inorganic pyrophosphatase in the genome of an apparently pre-luca extremophile, the archaeon Candidatus Korarchaeum cryptofilum.Journal of molecular evolution · 2014Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane-bound Na(+)-pyrophosphatase (Na(+)-PPase), working in parallel with the corresponding ATP-energized pumps, catalyzes active Na(+) transport in bacteria and archaea. Each ~75-kDa subunit of homodimeric Na(+)-PPase forms an unusual funnel-like structure with a catalytic site in the cytoplasmic part and a hydrophilic gated channel in the membrane. Here, we show that at subphysiological Na(+) concentrations (<5 mM), the Na(+)-PPases of Chlorobium limicola, four other bacteria, and one archaeon additionally exhibit an H(+)-pumping activity in inverted membrane vesicles prepared from recombinant Escherichia coli strains. H(+) accumulation in vesicles was measured with fluorescent pH indicators. At pH 6.2-8.2, H(+) transport activity was high at 0.1 mM Na(+) but decreased progressively with increasing Na(+) concentrations until virtually disappearing at 5 mM Na(+). In contrast, (22)Na(+) transport activity changed little over a Na(+) concentration range of 0.05-10 mM. Conservative substitutions of gate Glu(242) and nearby Ser(243) and Asn(677) residues reduced the catalytic and transport functions of the enzyme but did not affect the Na(+) dependence of H(+) transport, whereas a Lys(681) substitution abolished H(+) (but not Na(+)) transport. All four substitutions markedly decreased PPase affinity for the activating Na(+) ion. These results are interpreted in terms of a model that assumes the presence of two Na(+)-binding sites in the channel: one associated with the gate and controlling all enzyme activities and the other located at a distance and controlling only H(+) transport activity. The inherent H(+) transport activity of Na(+)-PPase provides a rationale for its easy evolution toward specific H(+) transport.
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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.