Archaeorhodopsin initially called bacteriorhodopsin, is responsible for chlorophyll independent photosynthesis. The protein in the retina, the main photosynthetic protein of the archaeon Halobacterium Salinarum is called Archaeorhodopsin.
It transforms green light energy (500–650 nm, maximum 568 nm) into an electrochemical proton gradient, which is then utilized by ATP synthase to produce ATP. It demonstrates vectorial catalysis and serves as a light-driven proton pump that transports protons out of the cell.
A 27 kDa integral membrane protein called "purple membrane," which can cover nearly 50% of the surface area of the archaeal cell, is known as Archaeorhodopsin. It is typically found in these two-dimensional crystalline patches.
Three identical protein chains are arranged in a hexagonal lattice and rotated by 120 degrees from one another to form the repeating structure. Seven transmembrane alpha helices and a two-stranded beta strand facing extracellularly are present in each monomer.
Bacterio-opsin, a protein precursor that is used in the synthesis of Archaeorhodopsin, is extensively altered after translation.
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