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- Weber, Joachim, et al. Show all 3 Authors
- Biochimica et biophysica acta 2019 v.1860 no.8 pp. 679-687
- Escherichia coli; H+/K+-exchanging ATPase; H-transporting ATP synthase; catalytic activity; energy; energy metabolism; glutamine; hydrogen bonding; hydrolysis; moieties; molecular dynamics; mutants; mutation; simulation models
- ... Functioning as a nanomotor, ATP synthase plays a vital role in the cellular energy metabolism. Interactions at the rotor and stator interface are critical to the energy transmission in ATP synthase. From mutational studies, we found that the γC87K mutation impairs energy coupling between proton translocation and nucleotide synthesis/hydrolysis. An additional glutamine mutation at γR242 (γR242Q) ca ...
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- Weber, Joachim, et al. Show all 4 Authors
- Journal of basic microbiology 2015 v.55 no.11 pp. 1245-1254
- Escherichia coli; Methylobacterium; active sites; amino acid sequences; amino acids; bacteria; biodegradation; biopolymers; carbon; carboxylesterase; chemotaxonomy; cypermethrin; genes; molecular cloning; molecular weight; open reading frames; phylogeny; proteins; pyrethrins; ribosomal RNA; sequence analysis
- ... A novel mesophilic bacterial strain, designated A‐1, was isolated from microbially contaminated biopolymer microcapsules. The bacterium was able to withstand and grow in liquid cultures supplemented with the pyrethroid cypermethrin in concentrations up to 400 mg L⁻¹. Furthermore, strain A‐1 could use cypermethrin as sole carbon source and could degrade >50% of it in 12 h. Based on phenotypic and c ...
- Weber, Joachim, et al. Show all 2 Author
- Proceedings of the National Academy of Sciences of the United States of America 2007 v.104 no.47 pp. 18478-18483
- H+/K+-exchanging ATPase; H-transporting ATP synthase; X-radiation; active sites; adenosine triphosphate; binding capacity; binding sites; catalytic activity; energy transfer; fluorescence; hydrolysis; prediction; tryptophan
- ... ATP synthase uses a unique rotary mechanism to couple ATP synthesis and hydrolysis to transmembrane proton translocation. The F₁ subcomplex has three catalytic nucleotide binding sites, one on each β subunit, with widely differing affinities for MgATP or MgADP. During rotational catalysis, the sites switch their affinities. The affinity of each site is determined by the position of the central γ s ...
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