ArticleBiophysical journal2006
Chemical modification of the bacterial porin OmpF: gain of selectivity by volume reduction.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Quantitative assessment of porin-mediated solute transport in biomimetic membranes.Applied microbiology and biotechnology · 2025Article
- Deamidated Human Triosephosphate Isomerase is a Promising Druggable Target.Biomolecules · 2020Article
- Electroosmosis Dominates Electrophoresis of Antibiotic Transport Across the Outer Membrane Porin F.Biophysical journal · 2020Article
- On the different sources of cooperativity in pH titrating sites of a membrane protein channel.The European physical journal. E, Soft matter · 2016Article
- A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations.Journal of the American Chemical Society · 2013Article
- Interacting ions in biophysics: real is not ideal.Biophysical journal · 2013Review
- Ionizable side chains at catalytic active sites of enzymes.European biophysics journal : EBJ · 2012Article
- Single-channel measurements of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli.European biophysics journal : EBJ · 2012Article
- Divalent Metal Ion Transport across Large Biological Ion Channels and Their Effect on Conductance and Selectivity.Biochemistry research international · 2012Article
- The ionization state of D37 in E. coli porin OmpF and the nature of conductance fluctuations in D37 mutants.European biophysics journal : EBJ · 2010Article
- Simulations of calcium channel block by trivalent cations: Gd(3+) competes with permeant ions for the selectivity filter.Biochimica et biophysica acta · 2010Article
- Multiple Scales in the Simulation of Ion Channels and Proteins.The journal of physical chemistry. C, Nanomaterials and interfaces · 2010Article
- Ionic partition and transport in multi-ionic channels: a molecular dynamics simulation study of the OmpF bacterial porin.Biophysical journal · 2010Article
- Energy variational analysis of ions in water and channels: Field theory for primitive models of complex ionic fluids.The Journal of chemical physics · 2010Article
- Comparing the temperature-dependent conductance of the two structurally similar E. coli porins OmpC and OmpF.Biophysical journal · 2010Article
- Protein structure and ionic selectivity in calcium channels: selectivity filter size, not shape, matters.Biochimica et biophysica acta · 2009Article
- Ions and inhibitors in the binding site of HIV protease: comparison of Monte Carlo simulations and the linearized Poisson-Boltzmann theory.Biophysical journal · 2009Article
- Diffusion, exclusion, and specific binding in a large channel: a study of OmpF selectivity inversion.Biophysical journal · 2009Article
- Engineering channels: atomic biology.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Energetics of divalent selectivity in a calcium channel: the ryanodine receptor case study.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
OmpF is an essentially nonselective porin isolated from the outer membrane of Escherichia coli. Here we report on the manipulation of the ion selectivity of OmpF by chemical modification with MTS reagents (MTSET, MTSEA, and MTSES) and the (rather bulky) tripeptide glutathione, all cysteine specific. When recorded in a gradient of 0.1//1 M CaCl2 or 0.1//1 M NaCl, pH 7.4 solutions, measured reversal potentials of the most cation-selective modified mutants were (virtually) identical to the Nernst potential of Ca2+ or Na+. Compared to this full cation selectivity, the anion-selective modified mutants performed somewhat less but nevertheless showed high anion selectivity. We conclude that a low permanent charge in combination with a narrow pore can render the same selectivity as a highly charged but wider pore. These results favor the view that both the electrostatic potential arising form the fixed charge in the pore and the space available at the selectivity filter contribute to the charge selection (i.e., cation versus anion selectivity) of a biological ion channel.
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