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This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430.

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Contents 1 Rhodopsin 2 Structure 3 Function 4 References

Rhodopsin

Bacteriorhodopsin is a photoreceptor protein found in Archaea. When in the presence of light energy and protons, the protein undergoes a conformational change and pumps protons out of the cell, creating an electrochemical gradient with a more negative intracellular environment ^[1].

Structure

The protein's main structure is .

Light energy and protonation of the molecule leads to a complex system of isomerization that releases a proton outside of the membrane. 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 ^[2].

Function

, where it reacts in the presence of light. This proton pump is used to create a gradient that can be used for things like ATP synthesis.

References

1. ↑ 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
2. ↑ 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