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CORRECTION article

Front. Plant Sci., 19 December 2016
Sec. Plant Physiology
Volume 7 - 2016 | https://doi.org/10.3389/fpls.2016.01888
This article is part of the Research Topic Aquaporins: dynamic role and regulation View all 15 articles

Corrigendum: Increased Permeability of the Aquaporin SoPIP2;1 by Mercury and Mutations in Loop A

This article is a correction to:

  1. Increased Permeability of the Aquaporin SoPIP2;1 by Mercury and Mutations in Loop A

    1. Read original article
\r\nAndreas Kirscht&#x;Andreas Kirscht†Sabeen Survery&#x;Sabeen Survery†Per KjellbomPer KjellbomUrban Johanson*Urban Johanson*
  • Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Lund, Sweden

A corrigendum on
Increased Permeability of the Aquaporin SoPIP2;1 by Mercury and Mutations in Loop A

by Kirscht A., Survery S., Kjellbom P., and Johanson U. (2016) Front. Plant Sci. 7:1249. doi: 10.3389/fpls.2016.01249

In our Original Research article it was incorrectly stated that cadmium and mercury have a similar preference for hexagonal coordination. Although both cadmium and mercury can bind at octahedral (not hexagonal) coordination sites their coordination preferences are not similar (Rulisek and Vondrasek, 1998). Hence, the fourth sentence under the subheading “Mercury Binding Site” in the Discussion should read: “It is described as a second binding site for cadmium, but given the comparable size of the cations and that both are capable of forming an octahedral coordination geometry (Rulisek and Vondrasek, 1998), one could imagine that also mercury has a potential to bind.” The authors apologize for the mistake. This error does not change the scientific conclusions of the article in any way.

Conflict of Interest Statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

References

Rulisek, L., and Vondrasek, J. (1998) Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, Hg2+) in metalloproteins. J. Inorg. Biochem. 71, 115–127.

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Keywords: aquaporin, water channel, major intrinsic protein, Spinacia oleracea, tryptophan fluorescence

Citation: Kirscht A, Survery S, Kjellbom P and Johanson U (2016) Corrigendum: Increased Permeability of the Aquaporin SoPIP2;1 by Mercury and Mutations in Loop A. Front. Plant Sci. 7:1888. doi: 10.3389/fpls.2016.01888

Received: 21 November 2016; Accepted: 30 November 2016;
Published: 19 December 2016.

Edited and reviewed by: Rupesh Kailasrao Deshmukh, Laval University, Canada

Copyright © 2016 Kirscht, Survery, Kjellbom and Johanson. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Urban Johanson, dXJiYW4uam9oYW5zb25AYmlvY2hlbWlzdHJ5Lmx1LnNl

†Shared first authors.

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