Abstract
BLUF (blue light sensor using flavin) proteins are the blue light receptors that consist of flavin-binding BLUF domains and functional domains. Upon blue light excitation, the hydrogen bond network around the flavin chromophore changes, and the absorption spectrum in the visible region shifts to red. Light signal received in the BLUF domain is intramolecularly or intermolecularly transmitted to the functional region. In this review, the reactions of three BLUF proteins with similar EAL functional groups within the protein (BlrP1, and YcgF), or with a separated target protein (PapB) are described using time-resolved diffusion technique. The diffusion coefficients (D) of the BLUF domains did not significantly change upon photoexcitation, whereas those of the full-length proteins BlrP1 and YcgF and the PapB–PapA system significantly decreased. The changes in D should be due to diffusion-sensitive conformational changes (DSCC) that alter the friction of diffusion. The time constants of the major D changes of BlrP1 and PapB–PapA were similar (~ 20 ms), although the magnitude of the friction change depended on the proteins. Similarities and differences among the reactions of these proteins were clarified from the viewpoint of DSCC.
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References
Gomelsky, M., & Klug, G. (2002). BLUF: A novel FAD-binding domain involved in sensory transduction in microorganisms. Trends in Biochemical Sciences, 27(10), 497–500. https://doi.org/10.1016/S0968-0004(02)02181-3
Losi, A. (2007). Flavin-based blue-light photosensors: A photobiophysics update. Photochemistry and Photobiology, 83(6), 1283–1300. https://doi.org/10.1111/j.1751-1097.2007.00196.x
Masuda, S. (2013). Light detection and signal transduction in the BLUF photoreceptors. Plant and Cell Physiology, 54(2), 171–179. https://doi.org/10.1093/pcp/pcs173
Park, S. Y., & Tame, J. R. H. (2017). Seeing the light with BLUF proteins. Biophysical Reviews, 9(2), 169–176. https://doi.org/10.1007/s12551-017-0258-6
Fujisawa, T., & Masuda, S. (2018). Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins. Biophysical Reviews, 10(2), 327–337. https://doi.org/10.1007/s12551-017-0355-6
Kita, A., Okajima, K., Morimoto, Y., Ikeuchi, M., & Miki, K. (2005). Structure of a cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue light sensor domain. Journal of Molecular Biology, 349(1), 1–9. https://doi.org/10.1016/J.JMB.2005.03.067
Anderson, S., Dragnea, V., Masuda, S., Ybe, J., Moffat, K., & Bauer, C. (2005). Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides. Biochemistry, 44(22), 7998–8005. https://doi.org/10.1021/BI0502691
Wu, Q., & Gardner, K. H. (2009). Structure and insight into blue light-induced changes in the BlrP1 BLUF domain. Biochemistry, 48(12), 2620–2629. https://doi.org/10.1021/bi802237r
Barends, T. R. M., Hartmann, E., Griese, J. J., Beitlich, T., Kirienko, N. V., Ryjenkov, D. A., et al. (2009). Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase. Nature, 459(7249), 1015–1018. https://doi.org/10.1038/nature07966
Jung, A., Domratcheva, T., Tarutina, M., Wu, Q., Ko, W. H., Shoeman, R. L., et al. (2005). Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction. Proceedings of the National Academy of Sciences of the United States of America, 102(35), 12350–12355. https://doi.org/10.1073/pnas.0500722102
Jung, A., Reinstein, J., Domratcheva, T., Shoeman, R. L., & Schlichting, I. (2006). Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction. Journal of Molecular Biology, 362(4), 717–732. https://doi.org/10.1016/j.jmb.2006.07.024
Chitrakar, I., Iuliano, J. N., He, Y. L., Woroniecka, H. A., Tolentino Collado, J., Wint, J. M., French, J. B., et al. (2020). structural basis for the regulation of biofilm formation and iron uptake in A. baumannii by the blue-light-using photoreceptor BIsA. ACS Infectious Diseases, 6(10), 2592–2603. https://doi.org/10.1021/acsinfecdis.0c00156
Yuan, H., Anderson, S., Masuda, S., Dragnea, V., Moffat, K., & Bauer, C. (2006). Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling. Biochemistry, 45(42), 12687–12694. https://doi.org/10.1021/bi061435n
Ohki, M., Sugiyama, K., Kawai, F., Tanaka, H., Nihei, Y., Unzai, S., et al. (2016). Structural insight into photoactivation of an adenylate cyclase from a photosynthetic cyanobacterium. Proceedings of the National Academy of Sciences of the United States of America, 113(24), 6659–6664. https://doi.org/10.1073/pnas.1517520113
Yin, L., Dragnea, V., Feldman, G., Hammad, L. A., Karty, J. A., Dann, C. E., & Bauer, C. E. (2013). Redox and light control the heme-sensing activity of AppA. MBio, 1, 1–10. https://doi.org/10.1128/MBIO.00563-13
Winkler, A., Heintz, U., Lindner, R., Reinstein, J., Shoeman, R. L., & Schlichting, I. (2013). A ternary AppA-PpsR-DNA complex mediates light regulation of photosynthesis-related gene expression. Nature structural & molecular biology, 20(7), 859–867. https://doi.org/10.1038/NSMB.2597
Lindner, R., Hartmann, E., Tarnawski, M., Winkler, A., Frey, D., Reinstein, J., et al. (2017). Photoactivation mechanism of a bacterial light-regulated adenylyl cyclase. Journal of molecular biology, 429(9), 1336–1351. https://doi.org/10.1016/J.JMB.2017.03.020
Grinstead, J. S., Hsu, S. T. D., Laan, W., Bonvin, A. M. J. J., Hellingwerf, K. J., Boelens, R., & Kaptein, R. (2006). The solution structure of the AppA BLUF domain: Insight into the mechanism of light-induced signaling. ChemBioChem, 7(1), 187–193. https://doi.org/10.1002/cbic.200500270
Conrad, K. S., Manahan, C. C., & Crane, B. R. (2014). Photochemistry of flavoprotein light sensors. Nature Chemical Biology, 10(10), 801–809. https://doi.org/10.1038/NCHEMBIO.1633
Fukushima, Y., Murai, Y., Okajima, K., Ikeuchi, M., & Itoh, S. (2008). Photoreactions of Tyr8- and Gln50-mutated BLUF domains of the PixD protein of Thermosynechococcus elongatus BP-1: Photoconversion at low temperature without Tyr8. Biochemistry, 47(2), 660–669. https://doi.org/10.1021/BI700674W
Goings, J. J., Li, P., Zhu, Q., & Hammes-Schiffer, S. (2020). Formation of an unusual glutamine tautomer in a blue light using flavin photocycle characterizes the light-adapted state. Proceedings of the National Academy of Sciences of the United States of America, 117(43), 26626–26632. https://doi.org/10.1073/PNAS.2016719117
Penzkofer, A., Stierl, M., Mathes, T., & Hegemann, P. (2014). Absorption and emission spectroscopic characterization of photo-dynamics of photoactivated adenylyl cyclase mutant bPAC-Y7F of Beggiatoa sp. Journal of Photochemistry and Photobiology B: Biology, 140, 182–193. https://doi.org/10.1016/J.JPHOTOBIOL.2014.06.017
Iwata, T., Nagai, T., Ito, S., Osoegawa, S., Iseki, M., Watanabe, M., et al. (2018). Hydrogen bonding environments in the photocycle process around the flavin chromophore of the AppA–BLUF domain. Journal of the American Chemical Society, 140(38), 11982–11991. https://doi.org/10.1021/JACS.8B05123
Dragnea, V., Arunkumar, A. I., Lee, C. W., Giedroc, D. P., & Bauer, C. E. (2010). A Q63E rhodobacter sphaeroides AppA BLUF domain mutant is locked in a pseudo-light-excited signaling state. Biochemistry, 49(50), 10682–10690. https://doi.org/10.1021/BI1002162
Khrenova, M. G., Nemukhin, A. V., & Domratcheva, T. (2013). Photoinduced electron transfer facilitates tautomerization of the conserved signaling glutamine side chain in BLUF protein light sensors. Journal of Physical Chemistry B, 117(8), 2369–2377. https://doi.org/10.1021/JP312775X
Hsiao, Y. W., Götze, J. P., & Thiel, W. (2012). The central role of Gln63 for the hydrogen bonding network and UV–visible spectrum of the AppA BLUF domain. Journal of Physical Chemistry B, 116(28), 8064–8073. https://doi.org/10.1021/JP3028758
Udvarhelyi, A., & Domratcheva, T. (2013). Glutamine rotamers in BLUF photoreceptors: A mechanistic reappraisal. Journal of Physical Chemistry B, 117(10), 2888–2897. https://doi.org/10.1021/JP400437X
Sadeghian, K., Bocola, M., & Schütz, M. (2008). A conclusive mechanism of the photoinduced reaction cascade in blue light using flavin photoreceptors. Journal of the American Chemical Society, 130(37), 12501–12513. https://doi.org/10.1021/JA803726A
Mathes, T., Van Stokkum, I. H. M., Bonetti, C., Hegemann, P., & Kennis, J. T. M. (2011). The hydrogen-bond switch reaction of the blrb bluf domain of rhodobacter sphaeroides. Journal of Physical Chemistry B, 115(24), 7963–7971. https://doi.org/10.1021/JP201296M
Bonetti, C., Stierl, M., Mathes, T., Van Stokkum, I. H. M., Mullen, K. M., Cohen-Stuart, T. A., et al. (2009). The role of key amino acids in the photoactivation pathway of the Synechocystis Slr1694 BLUF domain. Biochemistry, 48(48), 11458–11469. https://doi.org/10.1021/BI901196X
Domratcheva, T., Hartmann, E., Schlichting, I., & Kottke, T. (2016). Evidence for tautomerisation of glutamine in BLUF blue light receptors by vibrational spectroscopy and computational chemistry. Scientific Reports. https://doi.org/10.1038/SREP22669
Bonetti, C., Mathes, T., Van Stokkum, I. H. M., Mullen, K. M., Groot, M. L., Van Grondelle, R., et al. (2008). Hydrogen bond switching among flavin and amino acid side chains in the BLUF photoreceptor observed by ultrafast infrared spectroscopy. Biophysical Journal, 95(10), 4790–4802.
Götze, J. P., Greco, C., Mitrić, R., Bonačić-Koutecký, V., & Saalfrank, P. (2012). BLUF hydrogen network dynamics and UV/Vis spectra: A combined molecular dynamics and quantum chemical study. Journal of Computational Chemistry, 33(28), 2233–2242. https://doi.org/10.1002/JCC.23056
Toh, K. C., Van Stokkum, I. H. M., Hendriks, J., Alexandre, M. T. A., Arents, J. C., Perez, M. A., et al. (2008). On the signaling mechanism and the absence of photoreversibility in the AppA BLUF domain. Biophysical Journal, 95(1), 312–321. https://doi.org/10.1529/biophysj.107.117788
Kennis, J. T., & Groot, M. L. (2007). Ultrafast spectroscopy of biological photoreceptors. Current Opinion in Structural Biology, 17(5), 623–630. https://doi.org/10.1016/j.sbi.2007.09.006
Stelling, A. L., Ronayne, K. L., Nappa, J., Tonge, P. J., & Meech, S. R. (2007). Ultrafast structural dynamics in BLUF domains: Transient infrared spectroscopy of AppA and its mutants. Journal of the American Chemical Society, 129(50), 15556–15564. https://doi.org/10.1021/ja074074n
Gauden, M., Yeremenko, S., Laan, W., Van Stokkum, I. H. M., Ihalainen, J. A., Van Grondelle, R., et al. (2005). Photocycle of the flavin-binding photoreceptor AppA, a bacterial transcriptional antirepressor of photosynthesis genes. Biochemistry, 44(10), 3653–3662. https://doi.org/10.1021/bi047359a
Lukacs, A., Zhao, R. K., Haigney, A., Brust, R., Greetham, G. M., Towrie, M., et al. (2012). Excited state structure and dynamics of the neutral and anionic flavin radical revealed by ultrafast transient mid-IR to visible spectroscopy. The Journal of Physical Chemistry B, 116(20), 5810–5818. https://doi.org/10.1021/jp2116559
Lukacs, A., Haigney, A., Brust, R., Zhao, R. K., Stelling, A. L., Clark, I. P., et al. (2011). Photoexcitation of the blue light using FAD photoreceptor AppA results in ultrafast changes to the protein matrix. Journal of the American Chemical Society, 133(42), 16893–16900. https://doi.org/10.1021/ja2060098
Haigney, A., Lukacs, A., Brust, R., Zhao, R. K., Towrie, M., Greetham, G. M., et al. (2012). Vibrational assignment of the ultrafast infrared spectrum of the photoactivatable flavoprotein AppA. The journal of Physical Chemistry. B, 116(35), 10722–10729. https://doi.org/10.1021/jp305220m
Brust, R., Haigney, A., Lukacs, A., Gil, A., Hossain, S., Addison, K., et al. (2014). Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii. The Journal of Physical Chemistry Letters, 5(1), 220–224. https://doi.org/10.1021/jz4023738
Fujisawa, T., Takeuchi, S., Masuda, S., & Tahara, T. (2014). Signaling-state formation mechanism of a BLUF protein PapB from the purple bacterium Rhodopseudomonas palustris studied by femtosecond time-resolved absorption spectroscopy. Journal of Physical Chemistry B, 118(51), 14761–14773. https://doi.org/10.1021/jp5076252
Fujisawa, T., Masuda, S., Takeuchi, S., & Tahara, T. (2021). Femtosecond time-resolved absorption study of signaling state of a BLUF protein PixD from the cyanobacterium Synechocystis: Hydrogen-bond rearrangement completes during forward proton-coupled electron transfer. Journal of Physical Chemistry B, 125(44), 12154–12165. https://doi.org/10.1021/acs.jpcb.1c05957
Nakasone, Y., Ono, T. A., Ishii, A., Masuda, S., & Terazima, M. (2010). Temperature-sensitive reaction of a photosensor protein YcgF: Possibility of a role of temperature sensor. Biochemistry, 49(10), 2288–2296. https://doi.org/10.1021/bi902121z
Hazra, P., Inoue, K., Laan, W., Hellingwerf, K. J., & Terazima, M. (2008). Energetics and role of the hydrophobic interaction during photoreaction of the BLUF domain of AppA. The Journal of Physical Chemistry B, 112(5), 1494–1501. https://doi.org/10.1021/jp0767314
Shibata, K., Nakasone, Y., & Terazima, M. (2022). Selective photoinduced dimerization and slow recovery of a BLUF domain of EB1. The Journal of Physical Chemistry B. https://doi.org/10.1021/acs.jpcb.1c10100
Tanaka, K., Nakasone, Y., Okajima, K., Ikeuchi, M., Tokutomi, S., & Terazima, M. (2012). Time-resolved tracking of interprotein signal transduction: Synechocystis PixD-PixE complex as a sensor of light intensity. Journal of the American Chemical Society, 134(20), 8336–8339. https://doi.org/10.1021/ja301540r
Shibata, K., Nakasone, Y., & Terazima, M. (2018). Photoreaction of BlrP1: The role of a nonlinear photo-intensity sensor. Physical Chemistry Chemical Physics, 20(12), 8133–8142. https://doi.org/10.1039/c7cp08436f
Tanaka, K., Nakasone, Y., Okajima, K., Ikeuchi, M., Tokutomi, S., & Terazima, M. (2011). A way to sense light intensity: Multiple-excitation of the BLUF photoreceptor TePixD suppresses conformational change. FEBS Letters, 585(5), 786–790. https://doi.org/10.1016/j.febslet.2011.02.003
Hazra, P., Inoue, K., Laan, W., Hellingwerf, K. J., & Terazima, M. (2006). Tetramer formation kinetics in the signaling state of AppA monitored by time-resolved diffusion. Biophysical Journal, 91(2), 654–661. https://doi.org/10.1529/biophysj.106.083915
Toyooka, T., Tanaka, K., Okajima, K., Ikeuchi, M., Tokutomi, S., & Terazima, M. (2011). Macromolecular crowding effects on reactions of TePixD (Tll0078). Photochemistry and Photobiology, 87(3), 584–589. https://doi.org/10.1111/j.1751-1097.2010.00849.x
Nakasone, Y., Kikukawa, K., Masuda, S., & Terazima, M. (2019). Time-resolved study of interprotein signaling process of a blue light sensor PapB–PapA complex. Journal of Physical Chemistry B, 123(15), 3210–3218. https://doi.org/10.1021/acs.jpcb.9b00196
Nakasone, Y., Ono, T. A., Ishii, A., Masuda, S., & Terazima, M. (2007). Transient dimerization and conformational change of a BLUF protein: YcgF. Journal of the American Chemical Society, 129(22), 7028–7035. https://doi.org/10.1021/ja065682q
Tanaka, K., Nakasone, Y., Okajima, K., Ikeuchi, M., Tokutomi, S., & Terazima, M. (2009). Oligomeric-state-dependent conformational change of the BLUF protein TePixD (Tll0078). Journal of Molecular Biology, 386(5), 1290–1300. https://doi.org/10.1016/j.jmb.2009.01.026
Tanaka, K., Nakasone, Y., Okajima, K., Ikeuchi, M., Tokutomi, S., & Terazima, M. (2011). Light-induced conformational change and transient dissociation reaction of the BLUF photoreceptor synechocystis PixD (Slr1694). Journal of Molecular Biology, 409(5), 773–785. https://doi.org/10.1016/j.jmb.2011.04.032
Römling, U., & Amikam, D. (2006). Cyclic di-GMP as a second messenger. Current Opinion in Microbiology, 9(2), 218–228. https://doi.org/10.1016/j.mib.2006.02.010
Schirmer, T., & Jenal, U. (2009). Structural and mechanistic determinants of c-di-GMP signalling. Nature Reviews. Microbiology, 7(10), 724–735. https://doi.org/10.1038/NRMICRO2203
Rajagopal, S., Key, J. M., Purcell, E. B., Boerema, D. J., & Moffat, K. (2004). Purification and initial characterization of a putative blue light regulated phosphodiesterase from Escherichia coli. Photochemistry and Photobiology. https://doi.org/10.1562/2004-06-16-ra-203
Tschowri, N., Busse, S., & Hengge, R. (2009). The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli. Genes and Development, 23(4), 522–534. https://doi.org/10.1101/gad.499409
Tschowri, N., Lindenberg, S., & Hengge, R. (2012). Molecular function and potential evolution of the biofilm-modulating blue light-signalling pathway of Escherichia coli. Molecular Microbiology, 85(5), 893–906. https://doi.org/10.1111/j.1365-2958.2012.08147.x
Kanazawa, T., Ren, S., Maekawa, M., Hasegawa, K., Arisaka, F., Hyodo, M., et al. (2010). Biochemical and physiological characterization of a BLUF protein-EAL protein complex involved in blue light-dependent degradation of cyclic diguanylate in the purple bacterium rhodopseudomonas palustris. Biochemistry, 49(50), 10647–10655. https://doi.org/10.1021/bi101448t
Schirmer, T. (2016). C-di-GMP synthesis: structural aspects of evolution, catalysis and regulation. Journal of Molecular Biology, 428(19), 3683–3701. https://doi.org/10.1016/J.JMB.2016.07.023
Unno, M., Kikuchi, S., & Masuda, S. (2010). Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy. Biophysical Journal, 98(9), 1949–1956. https://doi.org/10.1016/j.bpj.2010.01.007
Unno, M., Sano, R., Masuda, S., Ono, T. A., & Yamauchi, S. (2005). Light-induced structural changes in the active site of the BLUF domain in AppA by Raman spectroscopy. Journal of Physical Chemistry B, 109(25), 12620–12626. https://doi.org/10.1021/JP0522664
Masuda, S., Hasegawa, K., & Ono, T. A. (2005). Tryptophan at position 104 is involved in transforming light signal into changes of β-sheet structure for the signaling state in the BLUF domain of AppA. Plant and Cell Physiology, 46(12), 1894–1901. https://doi.org/10.1093/PCP/PCI208
Karadi, K., Kapetanaki, S. M., Raics, K., Pecsi, I., Kapronczai, R., Fekete, Z., et al. (2020). Functional dynamics of a single tryptophan residue in a BLUF protein revealed by fluorescence spectroscopy. Scientific Reports. https://doi.org/10.1038/s41598-020-59073-5
Dragnea, V., Arunkumar, A. I., Hua, Y., Giedroc, D. P., & Bauer, C. E. (2009). Spectroscopic studies of the AppA BLUF domain from Rhodobacter sphaeroides: Addressing movement of tryptophan 104 in the signaling state. Biochemistry, 48(42), 9969–9979. https://doi.org/10.1021/bi9009067
Gauden, M., Grinstead, J. S., Laan, W., Van Stokkum, I. H. M., Avila-Perez, M., Toh, K. C., et al. (2007). On the role of aromatic side chains in the photoactivation of BLUF domains. Biochemistry, 46(25), 7405–7415. https://doi.org/10.1021/bi7006433
Terazima, M. (2011). Time-dependent intermolecular interaction during protein reactions. Physical Chemistry Chemical Physics, 13(38), 16928–16940. https://doi.org/10.1039/c1cp21868a
Terazima, M. (2021). Spectrally silent protein reaction dynamics revealed by time-resolved thermodynamics and diffusion techniques. Accounts of Chemical Research, 54(9), 2238–2248. https://doi.org/10.1021/acs.accounts.1c00113
Kondoh, M., & Terazima, M. (2017). Conformational and intermolecular interaction dynamics of photolyase/cryptochrome proteins monitored by the time-resolved diffusion technique. Photochemistry and Photobiology, 93(1), 15–25. https://doi.org/10.1111/php.12681
Inoue, K., Baden, N., & Terazima, M. (2005). Diffusion coefficient and the secondary structure of poly-L-glutamic acid in aqueous solution. The Journal of Physical Chemistry B, 109(47), 22623–22628. https://doi.org/10.1021/JP052897Y
Cussler, E. L. (2009). Diffusion. Cambridge: Cambridge University Press. https://doi.org/10.1017/CBO9780511805134
Iwata, K., Terazima, M., & Masuhara, H. (2018). Novel physical chemistry approaches in biophysical researches with advanced application of lasers: Detection and manipulation. Biochimica et Biophysica Acta: General Subjects, 1862(2), 335–357. https://doi.org/10.1016/J.BBAGEN.2017.11.003
Terazima, M. (2021). Time-resolved detection of association/dissociation reactions and conformation changes in photosensor proteins for application in optogenetics. Biophysical Reviews, 13(6), 1053–1059. https://doi.org/10.1007/s12551-021-00868-9
Schroeder, C., Werner, K., Otten, H., Krätzig, S., Schwalbe, H., & Essen, L. O. (2008). Influence of a joining helix on the BLUF domain of the YcgF photoreceptor from Escherichia coli. ChemBioChem, 9(15), 2463–2473. https://doi.org/10.1002/cbic.200800280
Khrenova, M., Domratcheva, T., Grigorenko, B., & Nemukhin, A. (2011). Coupling between the BLUF and EAL domains in the blue light-regulated phosphodiesterase BlrP1. Journal of Molecular Modeling, 17(7), 1579–1586. https://doi.org/10.1007/s00894-010-0842-1
Ren, S., Sawada, M., Hasegawa, K., Hayakawa, Y., Ohta, H., & Masuda, S. (2012). A PixD–PapB chimeric protein reveals the function of the BLUF domain C-terminal α-helices for light signal transduction. Plant and Cell Physiology, 53(9), 1638–1647. https://doi.org/10.1093/pcp/pcs108
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., et al. (2021). Highly accurate protein structure prediction with AlphaFold. Nature, 596(7873), 583–589. https://doi.org/10.1038/S41586-021-03819-2
Winkler, A., Udvarhelyi, A., Hartmann, E., Reinstein, J., Menzel, A., Shoeman, R. L., & Schlichting, I. (2014). Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states. Journal of Molecular Biology, 426(4), 853–868. https://doi.org/10.1016/j.jmb.2013.11.018
Hasegawa, K., Masuda, S., & Ono, T. A. (2006). Light induced structural changes of a full-length protein and its BLUF domain in YcgF(Blrp), a blue-light sensing protein that uses FAD (BLUF). Biochemistry, 45(11), 3785–3793. https://doi.org/10.1021/bi051820x
Shibata, K., Nakasone, Y., & Terazima, M. (2021). Enzymatic activity of the blue light-regulated phosphodiesterase BlrP1 from Klebsiella pneumoniae shows a nonlinear dependence on light intensity. FEBS Letters, 595(10), 1473–1479. https://doi.org/10.1002/1873-3468.14073
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The authors acknowledge all authors who have contributed to the papers cited in this review. This work was supported by a Grant-in-aid for Scientific Research on Innovative Areas (research in a proposed research area) (Nos. JP20107003, and JP25102004) and a Grant-in-aid for Scientific Research (17H03008, 21H01885, 21K19218 to M.T. and 18H045522, 20H04708 to Y.N.) from MEXT/JSPS.
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This publication is dedicated to Prof. Silvia E. Braslavsky, a pioneer in photobiology and photobiophysics, on the occasion of her 80th birthday.
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Nakasone, Y., Terazima, M. Time-resolved diffusion reveals photoreactions of BLUF proteins with similar functional domains. Photochem Photobiol Sci 21, 493–507 (2022). https://doi.org/10.1007/s43630-022-00214-2
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DOI: https://doi.org/10.1007/s43630-022-00214-2