AI Article Synopsis
- LOV domains are photoreceptor proteins that respond to blue light via a flavin chromophore, leading to a reaction that forms a stable covalent bond with a cysteine.
- Ultrafast spectroscopy reveals that when the formed adduct absorbs near-UV light, the bond breaks, restoring the original blue-light-sensitive state within about 100 picoseconds.
- This indicates that the LOV2 domain acts as a reversible photochromic switch, allowing it to be toggled between states using different light wavelengths.
Article Abstract
Light, oxygen, or voltage (LOV) domains constitute a new class of photoreceptor proteins that are sensitive to blue light through a noncovalently bound flavin chromophore. Blue-light absorption by the LOV2 domain initiates a photochemical reaction that results in formation of a long-lived covalent adduct between a cysteine and the flavin cofactor. We have applied ultrafast spectroscopy on the photoaccumulated covalent adduct state of LOV2 and find that, upon absorption of a near-UV photon by the adduct state, the covalent bond between the flavin and the cysteine is broken and the blue-light-sensitive ground state is regained on an ultrafast time scale of 100 ps. We thus demonstrate that the LOV2 domain is a reversible photochromic switch, which can be activated by blue light and deactivated by near-UV light.
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