Sandbox Reserved 819: Difference between revisions

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Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2. In these membranes, three Archaerhodopsin-2 form a trimeric structure, capturing light energy and using it to move protons across the membrane out of the cell.The resulting proton gradient is subsequently converted into chemical energy. The trimerization increases the thermal stability of the protein aR2 in the claret membrane of Halorubrum sp. aus-2 and enlarges the pH range where the protein can keep its neutral purple conformation.The trimerization increases the efficiency of the proton pumping power, which is defined by the largest pH gradient that the proton pump can generate across the membrane. So, the trimeric structure is more efficient than the monomeric structure.

The trimeric structure functions as a light-driven proton pump thanks to a retinal molecule, called RET, which changes its conformation when absorbing a photon, resulting in a conformational change of the surrounding protein and the proton pumping action.

Sandbox Reserved 819: Difference between revisions

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Revision as of 15:53, 23 December 2013 view source Allan Bernard (talk \| contribs) 142 edits No edit summary ← Older edit		Revision as of 16:03, 23 December 2013 view source Allan Bernard (talk \| contribs) 142 edits No edit summary Newer edit →
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	Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2. In these membranes, three Archaerhodopsin-2 form a trimeric structure, capturing light energy and using it to move protons across the membrane out of the cell.The resulting proton gradient is subsequently converted into chemical energy. The trimerization increases the thermal stability of the protein aR2 in the claret membrane of Halorubrum sp. aus-2 and enlarges the pH range where the protein can keep its neutral purple conformation.The trimerization increases the efficiency of the proton pumping power, which is defined by the largest pH gradient that the proton pump can generate across the membrane. So, the trimeric structure is more efficient than the monomeric structure.		Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2. In these membranes, three Archaerhodopsin-2 form a trimeric structure, capturing light energy and using it to move protons across the membrane out of the cell.The resulting proton gradient is subsequently converted into chemical energy. The trimerization increases the thermal stability of the protein aR2 in the claret membrane of Halorubrum sp. aus-2 and enlarges the pH range where the protein can keep its neutral purple conformation.The trimerization increases the efficiency of the proton pumping power, which is defined by the largest pH gradient that the proton pump can generate across the membrane. So, the trimeric structure is more efficient than the monomeric structure.
			The trimeric structure functions as a light-driven proton pump thanks to a retinal molecule, called RET, which changes its conformation when absorbing a photon, resulting in a conformational change of the surrounding protein and the proton pumping action.