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Rhodopsin
Bacteriorhodopsin is found in Archaea, where it reacts in the presence of light. When hit by light and bound to a proton, the protein undergoes a conformational change and pumps protons out of the cell, creating an electrochemical gradient.
Structure
The protein's main structure is [1].
The is at the center of the protein and is bound to the alpha helices. In bacterial rhodopsin, the retinal functions as a proton pump by a conformation from all trans to cis-13. The goes from cis to trans when the retinal is hit by light, and this change pumps protons out of the cell.
Function
This proton pump is used to create a gradient that can be used for things like ATP synthesis.
References
- ↑ Ernst OP, Lodowski DT, Elstner M, Hegemann P, Brown LS, Kandori H. Microbial and animal rhodopsins: structures, functions, and molecular mechanisms. Chem Rev. 2014 Jan 8;114(1):126-63. doi: 10.1021/cr4003769. Epub 2013 Dec 23. PMID:24364740 doi:http://dx.doi.org/10.1021/cr4003769
