Bacteriorhodopsin

Bacteriorhodopsin - a membrane protein of microorganisms belonging to the class Halobacteria, which are representatives of archaea. This protein performs the same function as chlorophyll in other organisms - it converts the energy of sunlight to the energy of chemical bonds. It acts as a light-dependent proton pump. Absorption of the quantum of light leads to rapid structural changes in the molecule, due to which the cation of hydrogen is transferred from the cytoplasm to the outer side of the cell membrane, after which the bacteriorodopsin molecule returns to its original state. The electrochemical potential due to the proton gradient is used by the cell for ATP synthesis, as well as for the transport of metabolites across the membrane, motion of flagella, etc.
The protein consists of 248 amino acid residues, with a molecular weight of about 26,000 Prosthetic group (non-cellular) to the lysine amino acid located at position 216. It may be one of two retinal isomers: one has all the double bonds in a trans configuration, the other in position 13 has a cis configuration. In bacteria, the ratio of molecules to different prosthetic groups is 1: 1. Bacterirodopsin is used to study proton transport in cells. Research into its use in holography and computing is also being conducted.

Bacteriorodopsin
A. V. Finkelstein, O. B. Ptitsyn, "Protein Physics", 2002


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