From 2011.igem.org
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| - | <h1>Principle</h1><p> <img style="float:right;" src="https://static.igem.org/mediawiki/2011/b/bc/Pr_glycoloyis.jpg" width="300px" height="224px"/> | + | <p> Yet to be put up </p> |
| - | <font color="#00FF00"><b>Proteorhodopsin(PR)</b></font>is a light driven proton pump, i.e. it pumps out <font color="#00FF00"><b>H+</b></font> ions across the bacterial membrane and hence alters the proton motive force of the cell membrane. It is native to marine bacteria and archaebacteria, where it serves to provide energy for bacterial metabolism and flagellar movement in extreme conditions.<br/><br/>
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| - | ATP synthase, the membrane proton channel coupled with ATP synthesis, uses up proton gradient to drive <font color="#00FF00"><b>phosphorylation</b></font> of ADP to give ATP, the energy molecule of the cell. The proton gradient for ATP synthase is generally provided by the activity of <font color="#00FF00"><b>Electron Transport Chain (ETC)</b></font> system. In case of proteorhodopsin expressing cells, PR gets activated when light of appropriate wavelength (<font color="#00FF00"><b>525</b></font> nm in case of Green light absorbing ProteoRhodopsin) is incident on the bacterial membrane, and it pumps out protons. Through this pumping action, the proton gradient across the cell membrane increases. The proton gradient developed by Proteorhodopsin is used up to drive ATP synthesis and hence increase the energy content of the cell. The <font color="#00FF00"><b>Proteorhodopsin + ATP synthase</b></font> system hence acts as a light based energy source for bacteria, which is analogous to Photophosphorylation in chloroplasts.<br/><br/>
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| - | Expression of PR in cells provides an energy advantage to cells, especially in conditions where the Electron Transport Chain is not fully functional. This energy advantage in terms of extra ATP has been proposed to be useful in improving global protein production, cell survivability in decreased substrate availability and other stress conditions, etc.
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Revision as of 12:40, 5 October 2011
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