ArticleBiophysical journal2010
Molecular mechanisms of how mercury inhibits water permeation through aquaporin-1: understanding by molecular dynamics simulation.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 87 citations in OpenAlex.
- A pan-vertebrate signaling motif controls the molecular function of intracellular AQP12.The Journal of cell biology · 2026Article
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- Cysteamine Chemisorption at Mercury-Solution Interfaces in the Context of Redox and Microdissociation Equilibria.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Deciphering Molecular Mechanisms Involved in the Modulation of Human Aquaporins' Water Permeability by Zinc Cations: A Molecular Dynamics Approach.International journal of molecular sciences · 2024Article
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Transport Characteristics of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Salinity Tolerance of Halophytic GrassInternational journal of molecular sciences · 2022Article
- Relevance of Aquaporins for Gamete Function and Cryopreservation.Animals : an open access journal from MDPI · 2022Review
- Experimental and conceptual approaches to root water transport.Plant and soil · 2022Review
- Aquaporins Are Essential to Maintain Motility and Membrane Lipid Architecture During Mammalian Sperm Capacitation.Frontiers in cell and developmental biology · 2021Article
- Transport of Reactive Oxygen and Nitrogen Species across Aquaporin: A Molecular Level Picture.Oxidative medicine and cellular longevity · 2019Article
- Review
- Characterization of acetate transport in colorectal cancer cells and potential therapeutic implications.Oncotarget · 2016Article
- Changes in Air CO₂ Concentration Differentially Alter Transcript Levels of NtAQP1 and NtPIP2;1 Aquaporin Genes in Tobacco Leaves.International journal of molecular sciences · 2016Article
- Phylogenomic and functional analyses of salmon lice aquaporins uncover the molecular diversity of the superfamily in Arthropoda.BMC genomics · 2015Article
- Aquaporin 1 Is Involved in Acid Secretion by Ionocytes of Zebrafish Embryos through Facilitating CO2 Transport.PloS one · 2015Article
- Molecular dynamics of water in the neighborhood of aquaporins.European biophysics journal : EBJ · 2013Review
- Human AQP1 is a constitutively open channel that closes by a membrane-tension-mediated mechanism.Biophysical journal · 2013Article
- Insights into the mechanisms of the selectivity filter of Escherichia coli aquaporin Z.Journal of molecular modeling · 2012Article
- Mercury inhibits the L170C mutant of aquaporin Z by making waters clog the water channel.Biophysical chemistry · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin (AQP) functions as a water-conducting pore. Mercury inhibits the water permeation through AQP. Although site-directed mutagenesis has shown that mercury binds to Cys189 during the inhibition process, it is not fully understood how this inhibits the water permeation through AQP1. We carried out 40 ns molecular dynamics simulations of bovine AQP1 tetramer with mercury (Hg-AQP1) or without mercury (Free AQP1). In Hg-AQP1, Cys191 (Cys189 in human AQP1) is converted to Cys-SHg+ in each monomer. During each last 10 ns, we observed water permeation events occurred 23 times in Free AQP1 and never in Hg-AQP1. Mercury binding did not influence the whole structure, but did induce a collapse in the orientation of several residues at the ar/R region. In Free AQP1, backbone oxygen atoms of Gly190, Cys191, and Gly192 lined, and were oriented to, the surface of the water pore channel. In Hg-AQP1, however, the SHg+ of Cys191-SHg+ was oriented toward the outside of the water pore. As a result, the backbone oxygen atoms of Gly190, Cys191, and Gly192 became disorganized and the ar/R region collapsed, thereby obstructing the permeation of water. We suggest that mercury disrupts the water pore of AQP1 through local conformational changes in the ar/R region.
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