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Volumn 69, Issue 1, 2005, Pages 252-254

Regeneration of bacteriorhodopsin from thermally unfolded bacterio-opsin and all-trans retinal at high temperatures

Author keywords

Bacterio opsin; Bacteriorhodopsin; Regeneration; Retinal; Structural fluctuation

Indexed keywords

HIGH TEMPERATURE APPLICATIONS; PROTEINS; THERMAL EFFECTS;

EID: 15244346657     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.69.252     Document Type: Article
Times cited : (6)

References (17)
  • 1
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi, J. K., Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem., 272, 31209-31212 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31209-31212
    • Lanyi, J.K.1
  • 2
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • Haupts, U., Tittor, J., and Oesterhelt, D., Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu. Rev. Biophys. Biomol. Struct., 28, 367-399 (1999).
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 3
    • 0016259151 scopus 로고
    • Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: Demonstration of an apo-membrane
    • Oesterhelt, D., Schuhmann, L., and Gruber, H., Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: demonstration of an apo-membrane. FEBS Lett., 44, 257-261 (1974).
    • (1974) FEBS Lett. , vol.44 , pp. 257-261
    • Oesterhelt, D.1    Schuhmann, L.2    Gruber, H.3
  • 4
    • 0016205756 scopus 로고
    • Reconstitution of bacteriorhodopsin
    • Oesterhelt, D., and Schuhmann, L., Reconstitution of bacteriorhodopsin. FEBS Lett., 44, 262-265 (1974).
    • (1974) FEBS Lett. , vol.44 , pp. 262-265
    • Oesterhelt, D.1    Schuhmann, L.2
  • 5
    • 0017377436 scopus 로고
    • Studies on the retinal-protein interaction in bacteriorhodopsin
    • Schreckenbach, T., Walckhoff, B., and Oesterhelt, D., Studies on the retinal-protein interaction in bacteriorhodopsin. Eur. J. Biochem., 76, 499-511 (1977).
    • (1977) Eur. J. Biochem. , vol.76 , pp. 499-511
    • Schreckenbach, T.1    Walckhoff, B.2    Oesterhelt, D.3
  • 6
    • 0001386064 scopus 로고
    • Removal of methyl groups from retinal controls the activity of bacteriorhodopsin
    • Gaertner, W., Towner, P., Hopf, H., and Oesterhelt, D., Removal of methyl groups from retinal controls the activity of bacteriorhodopsin. Biochemistry, 22, 2637-2644 (1983).
    • (1983) Biochemistry , vol.22 , pp. 2637-2644
    • Gaertner, W.1    Towner, P.2    Hopf, H.3    Oesterhelt, D.4
  • 7
    • 0018805369 scopus 로고
    • Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient
    • Rehorek, M., and Heyn, M. P., Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient. Biochemistry, 18, 4977-4983 (1979).
    • (1979) Biochemistry , vol.18 , pp. 4977-4983
    • Rehorek, M.1    Heyn, M.P.2
  • 8
    • 0343853021 scopus 로고    scopus 로고
    • Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier-transform infrared spectroscopy
    • Rudiger, M., Tittor, J., Gerwert, K., and Oesterhelt, D., Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier-transform infrared spectroscopy. Biochemistry, 36, 4867-4874 (1997).
    • (1997) Biochemistry , vol.36 , pp. 4867-4874
    • Rudiger, M.1    Tittor, J.2    Gerwert, K.3    Oesterhelt, D.4
  • 9
    • 0030612782 scopus 로고    scopus 로고
    • Similarity of bacteriorhodopsin structural changes triggered by chromophore removal and light-driven proton transport
    • Ludlam, G. J., and Rothschild, K. J., Similarity of bacteriorhodopsin structural changes triggered by chromophore removal and light-driven proton transport. FEBS Lett., 407, 285-288 (1997).
    • (1997) FEBS Lett. , vol.407 , pp. 285-288
    • Ludlam, G.J.1    Rothschild, K.J.2
  • 10
    • 0026611771 scopus 로고
    • The role of retinal in the thermal stability of the purple membrane
    • Cladera, J., Galisteo, M. L., Sabes, M., Mateo, P. L., and Padros, E., The role of retinal in the thermal stability of the purple membrane. Eur. J. Biochem., 207, 581-585 (1992).
    • (1992) Eur. J. Biochem. , vol.207 , pp. 581-585
    • Cladera, J.1    Galisteo, M.L.2    Sabes, M.3    Mateo, P.L.4    Padros, E.5
  • 11
    • 0029990541 scopus 로고    scopus 로고
    • Analysis of conformational changes in bacteriorhodopsin upon retinal removal
    • Cladera, J., Torres, J., and Padros, E., Analysis of conformational changes in bacteriorhodopsin upon retinal removal. Biophys. J., 70, 2882-2887 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 2882-2887
    • Cladera, J.1    Torres, J.2    Padros, E.3
  • 12
    • 0017870745 scopus 로고
    • Phase transitions of the purple membranes of Halobacterium halobium
    • Jackson, M. B., and Sturtevant, J. M., Phase transitions of the purple membranes of Halobacterium halobium. Biochemistry, 17, 911-915 (1978).
    • (1978) Biochemistry , vol.17 , pp. 911-915
    • Jackson, M.B.1    Sturtevant, J.M.2
  • 13
    • 0002097215 scopus 로고
    • Phase transition of the purple membrane and the brown holomembrane. X-ray diffraction, circular dichroism spectrum and absorption spectrum studies
    • Hiraki, K., Hamanaka, T., Mitsui, T., and Kito, Y., Phase transition of the purple membrane and the brown holomembrane. X-ray diffraction, circular dichroism spectrum and absorption spectrum studies. Biochim. Biophys. Acta, 647, 18-28 (1981).
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 18-28
    • Hiraki, K.1    Hamanaka, T.2    Mitsui, T.3    Kito, Y.4
  • 14
    • 0036293239 scopus 로고    scopus 로고
    • Irreversible photobleaching of bacteriorhodopsin in a high-temperature intermediate state
    • Yokoyama, Y., Sonoyama, M., and Mitaku, S., Irreversible photobleaching of bacteriorhodopsin in a high-temperature intermediate state. J. Biochem., 131, 785-790 (2002).
    • (2002) J. Biochem. , vol.131 , pp. 785-790
    • Yokoyama, Y.1    Sonoyama, M.2    Mitaku, S.3
  • 15
    • 1042302803 scopus 로고    scopus 로고
    • Inhomogeneous stability of bacteriorhodopsin in purple membrane against photobleaching at high temperature
    • Yokoyama, Y., Sonoyama, M., and Mitaku, S., Inhomogeneous stability of bacteriorhodopsin in purple membrane against photobleaching at high temperature. Proteins, 54, 442-454 (2004).
    • (2004) Proteins , vol.54 , pp. 442-454
    • Yokoyama, Y.1    Sonoyama, M.2    Mitaku, S.3
  • 16
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D., and Stoeckenius, W., Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol., 31, 667-678 (1974).
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 17
    • 0029082532 scopus 로고
    • Interaction stabilizing tertiary structure of bacteriorhodopsin studied by denaturation experiments
    • Mitaku, S., Suzuki, K., Odashima, S., Ikuta, K., Suwa, M., Kukita, F., Ishikawa, M., and Itoh, H., Interaction stabilizing tertiary structure of bacteriorhodopsin studied by denaturation experiments. Proteins, 22, 350-362 (1995).
    • (1995) Proteins , vol.22 , pp. 350-362
    • Mitaku, S.1    Suzuki, K.2    Odashima, S.3    Ikuta, K.4    Suwa, M.5    Kukita, F.6    Ishikawa, M.7    Itoh, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.