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Volumn 43, Issue 47, 2004, Pages 14979-14986

Structural intermediate in the photocycle of a BLUF (sensor of blue light using FAD) protein Slr1694 in a cyanobacterium Synechocystis sp. PCC6803

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOCHEMISTRY; DEHYDRATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN BONDS; LIGHTING; ULTRAVIOLET RADIATION;

EID: 9744258714     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048671n     Document Type: Article
Times cited : (59)

References (22)
  • 1
    • 2442559284 scopus 로고    scopus 로고
    • Light-induced structural changes in a putative blue-light receptor with a novel FAD binding fold sensor of blue-light using FAD (BLUF); Slr1694 of Synechocystis sp. PCC6803
    • Masuda, S., Hasegawa, K., Ishii, A., and Ono, T. (2004) Light-induced structural changes in a putative blue-light receptor with a novel FAD binding fold sensor of blue-light using FAD (BLUF); Slr1694 of Synechocystis sp. PCC6803, Biochemistry 43, 5304-5313.
    • (2004) Biochemistry , vol.43 , pp. 5304-5313
    • Masuda, S.1    Hasegawa, K.2    Ishii, A.3    Ono, T.4
  • 2
    • 0036804709 scopus 로고    scopus 로고
    • BULF: A novel FAD-binding domain involved in sensory transdunction in microorganisms
    • Gomelsky, M., and Klug, G. (2002) BULF: A novel FAD-binding domain involved in sensory transdunction in microorganisms, Trends Biol. Sci. 27, 497-500.
    • (2002) Trends Biol. Sci. , vol.27 , pp. 497-500
    • Gomelsky, M.1    Klug, G.2
  • 3
    • 84889314737 scopus 로고    scopus 로고
    • The antirepressor AppA uses the novel flavin-binding BLUF domain as blue-light-absorbing photoreceptor to control photosystem synthesis
    • (Briggs, W. R., and Spudich, J., Eds.) Wiley-VCH Publishing, Weinheim, Germany, in press
    • Masuda, S., and Bauer, C. E. (2005) The antirepressor AppA uses the novel flavin-binding BLUF domain as blue-light-absorbing photoreceptor to control photosystem synthesis, in Handbook of Photosensory Receptors (Briggs, W. R., and Spudich, J., Eds.) Wiley-VCH Publishing, Weinheim, Germany, in press.
    • (2005) Handbook of Photosensory Receptors
    • Masuda, S.1    Bauer, C.E.2
  • 4
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • Masuda, S., and Bauer, C. E. (2002) AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides, Cell 110, 613-623.
    • (2002) Cell , vol.110 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 6
    • 9744224501 scopus 로고    scopus 로고
    • Comparative spectroscopic studies of sensor of blue-light using FAD (BLUF) proteins, AppA of Rhodobacter sphaeroides and YcgF of Escherichia coli
    • (van der Est, A., and Bruce, D., Eds.) Allen Press, KA, in press
    • Masuda, S., and Ono, T. (2004) Comparative spectroscopic studies of sensor of blue-light using FAD (BLUF) proteins, AppA of Rhodobacter sphaeroides and YcgF of Escherichia coli, in Photosynthesis: Fundamental Aspects to Global Perspectives (van der Est, A., and Bruce, D., Eds.) Allen Press, KA, in press.
    • (2004) Photosynthesis: Fundamental Aspects to Global Perspectives
    • Masuda, S.1    Ono, T.2
  • 7
    • 2442454713 scopus 로고    scopus 로고
    • Structural and functional analysis of a novel flavoprotein in cyanobacteria
    • Okajima, K., Yoshihara, S., Geng, X., Katayama, M., and Ikeuchi, M. (2003) Structural and functional analysis of a novel flavoprotein in cyanobacteria, Plant Cell Physiol. 44 suppl, 162.
    • (2003) Plant Cell Physiol. , vol.44 , Issue.SUPPL. , pp. 162
    • Okajima, K.1    Yoshihara, S.2    Geng, X.3    Katayama, M.4    Ikeuchi, M.5
  • 8
    • 1942519865 scopus 로고    scopus 로고
    • Blue light stimulates cyanobacterial motility via a cAMP signal transduction system
    • Terauchi, K., and Ohmori, M. (2004) Blue light stimulates cyanobacterial motility via a cAMP signal transduction system, Mol. Microbiol. 52, 303-309.
    • (2004) Mol. Microbiol. , vol.52 , pp. 303-309
    • Terauchi, K.1    Ohmori, M.2
  • 9
    • 0037984816 scopus 로고    scopus 로고
    • Spectroscopic and mutational analysis of the blue-light photoreceptor AppA: A novel photocycle involving flavin stacking with an aromatic amino acid
    • Kraft, B. J., Masuda, S., Kikuchi, J., Dragnea, V., Tollin, G., Zaleski, J. M., and Bauer, C. E. (2003) Spectroscopic and mutational analysis of the blue-light photoreceptor AppA: A novel photocycle involving flavin stacking with an aromatic amino acid, Biochemistry 42, 6726-6734.
    • (2003) Biochemistry , vol.42 , pp. 6726-6734
    • Kraft, B.J.1    Masuda, S.2    Kikuchi, J.3    Dragnea, V.4    Tollin, G.5    Zaleski, J.M.6    Bauer, C.E.7
  • 10
    • 0141844456 scopus 로고    scopus 로고
    • Initial characterisation of the primary photochemistry of AppA, a BLUF-domain containing transcriptional anti-repressor protein from Rhodobacter sphaeroides: A key role for reversible intra-molecular proton transfer from the FAD chromophore to a conserved tyrosine?
    • Laan, W., van der Host, M. A., van Stokkum, I. H., and Hellingwerf, K. J. (2003) Initial characterisation of the primary photochemistry of AppA, a BLUF-domain containing transcriptional anti-repressor protein from Rhodobacter sphaeroides: A key role for reversible intra-molecular proton transfer from the FAD chromophore to a conserved tyrosine? Photochem. Photobiol. 78, 290-297.
    • (2003) Photochem. Photobiol. , vol.78 , pp. 290-297
    • Laan, W.1    Van Der Host, M.A.2    Van Stokkum, I.H.3    Hellingwerf, K.J.4
  • 11
    • 1642453927 scopus 로고    scopus 로고
    • Photoreceptor proteins, "star actors of modern times": A review of the functional dynamics in the structure of representative members of six different photoreceptor families
    • van der Horst, M. A., and Hellingwerf, K. J. (2004) Photoreceptor proteins, "star actors of modern times": A review of the functional dynamics in the structure of representative members of six different photoreceptor families, Acc. Chem. Res. 37, 13-20.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 13-20
    • Van Der Horst, M.A.1    Hellingwerf, K.J.2
  • 14
    • 0037306223 scopus 로고    scopus 로고
    • Phot-LOV1: Photocycle of a blue-light receptor domain from the green alga Chlamydomonas reinhardtii
    • Kottke, T., Heberle, J., Hehn, D., Dick, B., and Hegemann, P. (2003) Phot-LOV1: Photocycle of a blue-light receptor domain from the green alga Chlamydomonas reinhardtii, Biophys. J. 84, 1192-1201.
    • (2003) Biophys. J. , vol.84 , pp. 1192-1201
    • Kottke, T.1    Heberle, J.2    Hehn, D.3    Dick, B.4    Hegemann, P.5
  • 15
    • 0037489440 scopus 로고    scopus 로고
    • Light-induced structural changes in the LOV2 domain of Adiantum Phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy
    • Iwata, T., Nozaki, D., Tokutomi, S., Kagawa, T., Wada, M., and Kandori, H. (2003) Light-induced structural changes in the LOV2 domain of Adiantum Phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy, Biochemistry 42, 8183-8191.
    • (2003) Biochemistry , vol.42 , pp. 8183-8191
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kagawa, T.4    Wada, M.5    Kandori, H.6
  • 16
    • 0038024617 scopus 로고    scopus 로고
    • Light-induced electron transfer in a cryptochrome blue-light photoreceptor
    • Giovani, B., Byrdin, M., Ahmad, M., and Brettel, K. (2003) Light-induced electron transfer in a cryptochrome blue-light photoreceptor, Nat. Struct. Biol. 10, 489-490.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 489-490
    • Giovani, B.1    Byrdin, M.2    Ahmad, M.3    Brettel, K.4
  • 17
    • 0037062577 scopus 로고    scopus 로고
    • Vibrational spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1
    • Swartz, T. E., Wenzel, P. J., Corchnoy, S. B., Briggs, W. R., and Bogomolni, R. A. (2002) Vibrational spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1, Biochemistry 41, 7183-7189.
    • (2002) Biochemistry , vol.41 , pp. 7183-7189
    • Swartz, T.E.1    Wenzel, P.J.2    Corchnoy, S.B.3    Briggs, W.R.4    Bogomolni, R.A.5
  • 19
    • 12244256754 scopus 로고    scopus 로고
    • Vibrational spectroscopy of an algal phot-LOV1 domain probes the molecular changes associated with blue-light reception
    • Ataka, K., Hegemann, P., and Heberle, J. (2003) Vibrational spectroscopy of an algal phot-LOV1 domain probes the molecular changes associated with blue-light reception, Biophys. J. 84, 466-474.
    • (2003) Biophys. J. , vol.84 , pp. 466-474
    • Ataka, K.1    Hegemann, P.2    Heberle, J.3
  • 20
    • 0037048688 scopus 로고    scopus 로고
    • Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum Phytochrom3
    • Iwata, T., Tokutomi, S., and Kandori, H. (2002) Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum Phytochrom3, J. Am. Chem. Soc. 124, 11840-11841.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11840-11841
    • Iwata, T.1    Tokutomi, S.2    Kandori, H.3
  • 21
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., Christie, J. M., Knieb, E., Lempert, U., and Briggs, W. R. (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin, Biochemistry 39, 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 22
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S., and Moffat, K. (2002) Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch, Plant Cell 14, 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.