The LOV2 domain of phototropin: A reversible photochromic switch

J.T.M. Kennis, N.H.M. van Stokkum, S. Crosson, M.L. Gauden, K. Moffat, R. van Grondelle

Research output: Contribution to JournalArticleAcademicpeer-review

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. Copyright © 2004 American Chemical Society.
Original languageEnglish
Pages (from-to)4512-4513
JournalJournal of the American Chemical Society
Volume126
Issue number14
DOIs
Publication statusPublished - 2004

Bibliographical note

The LOV2 domain of phototropin: A reversible photochromic switch

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