ArticleBiophysical chemistry2012
Mercury inhibits the L170C mutant of aquaporin Z by making waters clog the water channel.
Article in Biophysical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- Investigating the Mechanisms of AquaporinZ Reconstitution through Polymeric Vesicle Composition for a Biomimetic Membrane.Polymers · 2020Article
- Identification of AtHsp90.6 involved in early embryogenesis and its structure prediction by molecular dynamics simulations.Royal Society open science · 2019Article
- AThe Journal of biological chemistry · 2019Article
- Molecular dynamics simulation and bioinformatics study on chloroplast stromal ridge complex from rice (Oryza sativa L.).BMC bioinformatics · 2016Article
- Population shift between the open and closed states changes the water permeability of an Aquaporin Z mutant.Biophysical journal · 2012Article
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Authors and funding
3 authors.
Funding
Abstract
We conduct in silico experiments of the L170C mutant of the Escherichia coli aquaporin Z (AQPZ) with and without mercury bonded to residue Cys 170. We find that bonding mercury to Cys 170 does not induce consequential structural changes to the protein. We further find that mercury does not stick in the middle of the water channel to simply occlude water permeation, but resides on the wall of the water pore. However, we observe that the water permeation coefficient of L170C-Hg(+) (with one mercury ion bonded to Cys 170) is approximately half of that of the mercury-free L170C. We examine the interactions between the mercury ion and the waters in its vicinity and find that five to six waters are strongly attracted by the mercury ion, occluding the space of the water channel. Therefore we conclude that mercury, at low concentration, inhibits AQPZ-L170C mutant by making water molecules clog the water channel.
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