Variation in LOV photoreceptor activation dynamics probed by time-resolved infrared spectroscopy

Iuliano, James N., Gil, Agniezka A., Laptenok, Sergey P., Hall, Christopher R., Tolentino Collado, Jinnette, Lukacs, Andras, Ahmed, Safaa A. Hag, Abyad, Jenna, Daryaee, Taraneh, Greetham, Gregory M., Sazanovich, Igor V., Illarionov, Boris, Bacher, Adelbert, Fischer, Markus, Towrie, Michael, French, Jarrod B., Meech, Stephen R. ORCID: and Tonge, Peter J. (2018) Variation in LOV photoreceptor activation dynamics probed by time-resolved infrared spectroscopy. Biochemistry-US, 57 (5). 620–630.

[thumbnail of Accepted manuscript]
PDF (Accepted manuscript) - Accepted Version
Download (5MB) | Preview


The light, oxygen, voltage (LOV) domain proteins are blue light photoreceptors that utilize a non-covalently bound flavin mononucleotide (FMN) cofactor as the chromophore. The modular nature of these proteins has led to their wide adoption in the emerging fields of optogenetics and optobiology, where the LOV domain has been fused to a variety of output domains leading to novel light-controlled applications. In the present work, we extend our studies of the sub-picosecond to sub-millisecond transient infrared spectroscopy of the isolated LOV domain AsLOV2 to three full-length photoreceptors in which the LOV domain is fused to an output domain: the LOV-STAS protein, YtvA, the LOV-HTH transcription factor, EL222, and the LOV-histidine kinase, LovK. Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate. However significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain. While the rate of adduct formation varies by only 3.6-fold amongst the proteins, the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to sub-millisecond timescales and vary by orders of magnitude depending on the different output function of each LOV domain.

Item Type: Article
Uncontrolled Keywords: ultrafast infrared ,lov domain,flavoprotein,optogenetics
Faculty \ School: Faculty of Science > School of Chemistry
UEA Research Groups: Faculty of Science > Research Groups > Chemistry of Light and Energy
Faculty of Science > Research Groups > Centre for Photonics and Quantum Science
Depositing User: Pure Connector
Date Deposited: 19 Dec 2017 06:07
Last Modified: 09 Feb 2023 13:45
DOI: 10.1021/acs.biochem.7b01040


Downloads per month over past year

Actions (login required)

View Item View Item