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dc.contributor.authorIuliano, James N.
dc.contributor.authorGil, Agnieszka A.
dc.contributor.authorLaptenok, Siarhei
dc.contributor.authorHall, Christopher R.
dc.contributor.authorTolentino Collado, Jinnette
dc.contributor.authorLukacs, Andras
dc.contributor.authorHag Ahmed, Safaa A
dc.contributor.authorAbyad, Jenna
dc.contributor.authorDaryaee, Taraneh
dc.contributor.authorGreetham, Gregory M.
dc.contributor.authorSazanovich, Igor V.
dc.contributor.authorIllarionov, Boris
dc.contributor.authorBacher, Adelbert
dc.contributor.authorFischer, Markus
dc.contributor.authorTowrie, Michael
dc.contributor.authorFrench, Jarrod B.
dc.contributor.authorMeech, Stephen R.
dc.contributor.authorTonge, Peter J
dc.date.accessioned2017-12-21T13:57:05Z
dc.date.available2017-12-21T13:57:05Z
dc.date.issued2018-01-04
dc.identifier.citationIuliano JN, Gil AA, Laptenok SP, Hall CR, Tolentino Collado J, et al. (2017) Variation in LOV Photoreceptor Activation Dynamics Probed by Time Resolved Infrared Spectroscopy. Biochemistry. Available: http://dx.doi.org/10.1021/acs.biochem.7b01040.
dc.identifier.issn0006-2960
dc.identifier.issn1520-4995
dc.identifier.doi10.1021/acs.biochem.7b01040
dc.identifier.urihttp://hdl.handle.net/10754/626423
dc.description.abstractThe 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.
dc.description.sponsorshipWe 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.
dc.publisherAmerican Chemical Society (ACS)
dc.relation.urlhttp://pubs.acs.org/doi/10.1021/acs.biochem.7b01040
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/10.1021/acs.biochem.7b01040.
dc.subjectLOV domain
dc.subjectPhotoreceptor
dc.subjectUltrafast infrared
dc.subjectFlavoprotein
dc.subjectAsLOV2
dc.subjectYtvA
dc.subjectEL222
dc.subjectLovK
dc.titleVariation in LOV Photoreceptor Activation Dynamics Probed by Time Resolved Infrared Spectroscopy
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalBiochemistry
dc.eprint.versionPost-print
dc.contributor.institutionDepartment of Chemistry, Stony Brook University, New York, 11794, United States
dc.contributor.institutionSchool of Chemistry, University of East Anglia, Norwich, NR4 7TJ, U.K.
dc.contributor.institutionDepartment of Biophysics, Medical School, University of Pecs, Szigetiút 12, 7624 Pecs, HungaryǁCentral Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot, OX11 0QX, U.K.
dc.contributor.institutionDepartment Chemie, Technische Universität München, D-85747 Garching, Germany
dc.contributor.institutionInstitut für Biochemie und Lebensmittelchemie, Universität Hamburg, Grindelallee 117, D-20146 Hamburg, Germany
kaust.personLaptenok, Siarhei
refterms.dateFOA2018-12-14T00:00:00Z
dc.date.published-online2018-01-04
dc.date.published-print2018-02-06


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