Atypical mechanism of conduction in potassium channels
Potassium channels can conduct passively K⁺ ions with rates of up to [almost equal to]10⁸ ions per second at physiological conditions, and they are selective to these species by a factor of 10⁴ over Na⁺ ions. Ion conduction has been proposed to involve transitions between 2 main states, with 2 or 3...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2009-09, Vol.106 (38), p.16074-16077 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Furini, Simone Domene, Carmen |
| description | Potassium channels can conduct passively K⁺ ions with rates of up to [almost equal to]10⁸ ions per second at physiological conditions, and they are selective to these species by a factor of 10⁴ over Na⁺ ions. Ion conduction has been proposed to involve transitions between 2 main states, with 2 or 3 K⁺ ions occupying the selectivity filter separated by an intervening water molecule. The largest free energy barrier of such a process was reported to be of the order of 2-3 kcal mol⁻¹. Here, we present an alternative mechanism for conduction of K⁺ in potassium channels where site vacancies are involved, and we propose that coexistence of several ion permeation mechanisms is energetically possible. Conduction can be described as a more anarchic phenomenon than previously characterized by the concerted translocations of K⁺-water-K⁺. |
| doi_str_mv | 10.1073/pnas.0903226106 |
| format | Article |
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Ion conduction has been proposed to involve transitions between 2 main states, with 2 or 3 K⁺ ions occupying the selectivity filter separated by an intervening water molecule. The largest free energy barrier of such a process was reported to be of the order of 2-3 kcal mol⁻¹. Here, we present an alternative mechanism for conduction of K⁺ in potassium channels where site vacancies are involved, and we propose that coexistence of several ion permeation mechanisms is energetically possible. 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Conduction can be described as a more anarchic phenomenon than previously characterized by the concerted translocations of K⁺-water-K⁺.</description><subject>Amino acids</subject><subject>Atoms</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - physiology</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Computer Simulation</subject><subject>Conduction</subject><subject>Crystallography, X-Ray</subject><subject>Free energy</subject><subject>Ion Channel Gating</subject><subject>Ions</subject><subject>Models, Molecular</subject><subject>Molecular dynamics</subject><subject>Molecules</subject><subject>Physical Sciences</subject><subject>Potassium</subject><subject>Potassium - chemistry</subject><subject>Potassium channels</subject><subject>Potassium Channels - chemistry</subject><subject>Potassium Channels - physiology</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Sodium</subject><subject>Thermodynamics</subject><subject>Water</subject><subject>Water - chemistry</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEcxYModl09e1IHD4KHab_5PbkIpbQqFDxozyGTTdosM8k4yYj9782yS1e99BTI9_Nevi8PodcYTjFIejZFk09BASVEYBBP0AqDwq1gCp6iFQCRbccIO0Evct4CgOIdPEcnWHXAq2KFxHm5n4I1QzM6e2diyGOTfGNT3Cy2hBSbEJspFZNzWMZmh0Q35JfomTdDdq8O5xrdXF3-uPjSXn_7_PXi_Lq1gkBpuTIbC71kCvfeeGs4YDD1TvWd7Aklpq7OpPeiQpSxjWLemJ4RYL2XGOgafdr7Tks_uo11scxm0NMcRjPf62SC_ncSw52-Tb80kZxwrKrBh4PBnH4uLhc9hmzdMJjo0pK1kKLDVPBHQYIJoaBoBd__B27TMsf6C5oAZvVNJSt0tofsnHKenX9YGYPeNad3zeljc1Xx9u-kR_5QVQU-HoCd8mgnNO00FiCZ9sswFPe7VLZ5hK3Imz2yzSXNDwwD1nGoUdfo3X7uTdLmdg5Z33yvASlg0dWUnP4Bbse_3g</recordid><startdate>20090922</startdate><enddate>20090922</enddate><creator>Furini, Simone</creator><creator>Domene, Carmen</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7ST</scope><scope>7U6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090922</creationdate><title>Atypical mechanism of conduction in potassium channels</title><author>Furini, Simone ; 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Ion conduction has been proposed to involve transitions between 2 main states, with 2 or 3 K⁺ ions occupying the selectivity filter separated by an intervening water molecule. The largest free energy barrier of such a process was reported to be of the order of 2-3 kcal mol⁻¹. Here, we present an alternative mechanism for conduction of K⁺ in potassium channels where site vacancies are involved, and we propose that coexistence of several ion permeation mechanisms is energetically possible. Conduction can be described as a more anarchic phenomenon than previously characterized by the concerted translocations of K⁺-water-K⁺.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>19805261</pmid><doi>10.1073/pnas.0903226106</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Atoms Bacterial Proteins - chemistry Bacterial Proteins - physiology Binding Sites Biochemistry Biological Sciences Computer Simulation Conduction Crystallography, X-Ray Free energy Ion Channel Gating Ions Models, Molecular Molecular dynamics Molecules Physical Sciences Potassium Potassium - chemistry Potassium channels Potassium Channels - chemistry Potassium Channels - physiology Protein Conformation Protein Structure, Tertiary Sodium Thermodynamics Water Water - chemistry |
| title | Atypical mechanism of conduction in potassium channels |
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