AI Article Synopsis
- The first microbial rhodopsin, bacteriorhodopsin from Halobacterium salinarum, was discovered in 1971 and sparked significant advancements in membrane protein research.
- Until 1999, only a few types of archaeal rhodopsins were known, but the discovery of bacterial rhodopsin in 2000 opened the door to a new era of research.
- Rhodopsins are now known to exist across all life domains and even in viruses, demonstrating a wide variety of functions while maintaining similar structures, highlighting their scientific and technological potential.
Article Abstract
The first microbial rhodopsin, a light-driven proton pump bacteriorhodopsin from Halobacterium salinarum (HsBR), was discovered in 1971. Since then, this seven-α-helical protein, comprising a retinal molecule as a cofactor, became a major driver of groundbreaking developments in membrane protein research. However, until 1999 only a few archaeal rhodopsins, acting as light-driven proton and chloride pumps and also photosensors, were known. A new microbial rhodopsin era started in 2000 when the first bacterial rhodopsin, a proton pump, was discovered. Later it became clear that there are unexpectedly many rhodopsins, and they are present in all the domains of life and even in viruses. It turned out that they execute such a diversity of functions while being "nearly the same." The incredible evolution of the research area of rhodopsins and the scientific and technological potential of the proteins is described in the review with a focus on their function-structure relationships.
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| http://dx.doi.org/10.1007/978-1-0716-2329-9_1 | DOI Listing |
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