Variation in LOV Photoreceptor Activation Dynamics Probed by Time Resolved Infrared Spectroscopy

James N. Iuliano, Agnieszka A. Gil, Siarhei Laptenok, Christopher R. Hall, Jinnette Tolentino Collado, Andras Lukacs, Safaa A Hag Ahmed, Jenna Abyad, Taraneh Daryaee, Gregory M. Greetham, Igor V. Sazanovich, Boris Illarionov, Adelbert Bacher, Markus Fischer, Michael Towrie, Jarrod B. French, Stephen R. Meech, Peter J Tonge

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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 several hundred microsecond 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.
Original languageEnglish (US)
Pages (from-to)620-630
Number of pages11
Issue number5
StatePublished - Jan 4 2018
Externally publishedYes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: We are grateful to STFC for access to the ULTRA laser facility. We are grateful to Professor Ray Owens and Anil Verma for assistance in protein preparation and access to the Oxford Protein Production Facility-UK.


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