Function
Bacteriorhodopsin (Br) is a membrane protein in Archaea which moves protons across the cell membrane. See also Bacteriorhodopsin (Hebrew).
Halorhodopsin uses light energy to pump chloride through biological membranes in Haloarchaea[1].
Sensory rhodopsin uses light energy to pump calcium ions through biological membranes. They are ubiquitous and use retinal as their chromophore[2].
Xanthorhodopsin is a light-driven proton pump which uses the carotenoid salinixanthin as a second chromophore[3].
Archaerhodopsin responds to yellow or green light by pumping protons out of cells and are used as optogenetic tools[4].
Proteorhodopsins are the most abundant retinal-based photoreceptors. It is found in many marine bacteria[5].
Deltarhodopsin is a light-driven proton pump found in the archaebacteria Halloterrigena turkmenica[6].
Xenorhodopsin is an enigmatic new class of microbial rhodopsins[7].
Structural highlights
Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. The retinal interacts predominantly with hydrophobic and aromatic residues [8] (Hydrophobic, Polar).
3D Structures of bacteriorhodopsin
Bacteriorhodopsin 3D structures
- ↑ Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k
- ↑ Spudich JL. The multitalented microbial sensory rhodopsins. Trends Microbiol. 2006 Nov;14(11):480-7. doi: 10.1016/j.tim.2006.09.005. Epub, 2006 Sep 26. PMID:17005405 doi:https://dx.doi.org/10.1016/j.tim.2006.09.005
- ↑ Lanyi JK, Balashov SP. Xanthorhodopsin: a bacteriorhodopsin-like proton pump with a carotenoid antenna. Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):684-8. doi:, 10.1016/j.bbabio.2008.05.005. Epub 2008 May 16. PMID:18515067 doi:https://dx.doi.org/10.1016/j.bbabio.2008.05.005
- ↑ El-Gaby M, Zhang Y, Wolf K, Schwiening CJ, Paulsen O, Shipton OA. Archaerhodopsin Selectively and Reversibly Silences Synaptic Transmission through Altered pH. Cell Rep. 2016 Aug 23;16(8):2259-2268. doi: 10.1016/j.celrep.2016.07.057. Epub, 2016 Aug 11. PMID:27524609 doi:https://dx.doi.org/10.1016/j.celrep.2016.07.057
- ↑ Bamann C, Bamberg E, Wachtveitl J, Glaubitz C. Proteorhodopsin. Biochim Biophys Acta. 2014 May;1837(5):614-25. doi: 10.1016/j.bbabio.2013.09.010., Epub 2013 Sep 20. PMID:24060527 doi:https://dx.doi.org/10.1016/j.bbabio.2013.09.010
- ↑ Hara KY, Wada T, Kino K, Asahi T, Sawamura N. Construction of photoenergetic mitochondria in cultured mammalian cells. Sci Rep. 2013;3:1635. doi: 10.1038/srep01635. PMID:23567447 doi:https://dx.doi.org/10.1038/srep01635
- ↑ Ugalde JA, Podell S, Narasingarao P, Allen EE. Xenorhodopsins, an enigmatic new class of microbial rhodopsins horizontally transferred between archaea and bacteria. Biol Direct. 2011 Oct 10;6:52. doi: 10.1186/1745-6150-6-52. PMID:21985229 doi:https://dx.doi.org/10.1186/1745-6150-6-52
- ↑ Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k
