메뉴 건너뛰기




Volumn 64, Issue 18, 2007, Pages 2323-2328

Xanthorhodopsin: Proton pump with a carotenoid antenna

Author keywords

Carotenoid binding; Light energy transfer; Proton transport; Salinixanthin

Indexed keywords

BACTERIORHODOPSIN; CAROTENOID; PROTON PUMP; RETINOID BINDING PROTEIN; RHODOPSIN; UNCLASSIFIED DRUG; XANTHORHODOPSIN;

EID: 34548652250     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-7167-y     Document Type: Short Survey
Times cited : (38)

References (58)
  • 2
    • 33751541151 scopus 로고    scopus 로고
    • Functions of carotenoids in xanthorhodopsin and archaerhodopsin, from action spectra of photo-inhibition of cell respiration
    • Boichenko V. A., Wang J. M., Antón J., Lanyi J. K. and Balashov S. P. (2006) Functions of carotenoids in xanthorhodopsin and archaerhodopsin, from action spectra of photo-inhibition of cell respiration. Biochim. Biophys. Acta 1757, 1649-1656.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1649-1656
    • Boichenko, V.A.1    Wang, J.M.2    Antón, J.3    Lanyi, J.K.4    Balashov, S.P.5
  • 3
    • 33748500229 scopus 로고    scopus 로고
    • Induced chirality of light-harvesting carotenoid salinixanthin and its interaction with the retinal of xanthorhodopsin
    • Balashov S. P., Imasheva E. S. and Lanyi J. K. (2006) Induced chirality of light-harvesting carotenoid salinixanthin and its interaction with the retinal of xanthorhodopsin. Biochemistry 45, 10998-11004.
    • (2006) Biochemistry , vol.45 , pp. 10998-11004
    • Balashov, S.P.1    Imasheva, E.S.2    Lanyi, J.K.3
  • 5
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt D. and Stoeckenius W. (1971) Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature 233, 149-152.
    • (1971) Nature , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 6
    • 0020479529 scopus 로고
    • Halorhodopsin is a light-driven chloride pump
    • Schobert B. and Lanyi J. K. (1982) Halorhodopsin is a light-driven chloride pump. J. Biol. Chem. 257, 10306-10313.
    • (1982) J. Biol. Chem , vol.257 , pp. 10306-10313
    • Schobert, B.1    Lanyi, J.K.2
  • 7
    • 0000373165 scopus 로고
    • Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium
    • Bogomolni R. A. and Spudich J. L. (1982) Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium. Proc. Natl. Acad. Sci. USA 79, 6250-6254.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6250-6254
    • Bogomolni, R.A.1    Spudich, J.L.2
  • 8
    • 84982542707 scopus 로고    scopus 로고
    • Takahashi T., Tomioka H., Kamo N. and Kobatake Y. (1985)A photosystem other than PS370 also mediates the negative phototaxis of Halobacterium halobium. FEMS Microbiol. Lett. 28, 161-164.
    • Takahashi T., Tomioka H., Kamo N. and Kobatake Y. (1985)A photosystem other than PS370 also mediates the negative phototaxis of Halobacterium halobium. FEMS Microbiol. Lett. 28, 161-164.
  • 10
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt D. (1998) The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Cell Biol. 8, 489-500.
    • (1998) Curr. Opin. Cell Biol , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 14
    • 11144354360 scopus 로고    scopus 로고
    • Venter J. C., Remington K., Heidelberg J. F., Halpern A. L., Rusch D., Eisen J. A., Wu D., Paulsen I., Nelson K. E., Nelson W., Fouts D. E., Levy S. et al. (2004) Environmental genome shotgun sequencing of the Sargasso Sea. Science 304, 66-74.
    • Venter J. C., Remington K., Heidelberg J. F., Halpern A. L., Rusch D., Eisen J. A., Wu D., Paulsen I., Nelson K. E., Nelson W., Fouts D. E., Levy S. et al. (2004) Environmental genome shotgun sequencing of the Sargasso Sea. Science 304, 66-74.
  • 15
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: Structures and functions from archaea to humans
    • Spudich J. L., Yang C. S., Jung K. H. and Spudich E. N. (2000) Retinylidene proteins: structures and functions from archaea to humans. Annu. Rev. Cell. Dev. Biol. 16, 365-392.
    • (2000) Annu. Rev. Cell. Dev. Biol , vol.16 , pp. 365-392
    • Spudich, J.L.1    Yang, C.S.2    Jung, K.H.3    Spudich, E.N.4
  • 16
    • 18744369621 scopus 로고    scopus 로고
    • Leptosphaeria rhodopsin: Bacteriorhodopsin-like proton pump from a eukaryote
    • Waschuk S. A., Bezerra J., A. G., Shi L. and Brown L. S. (2005) Leptosphaeria rhodopsin: Bacteriorhodopsin-like proton pump from a eukaryote. Proc. Natl. Acad. Sci. USA 102, 6879-6883.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6879-6883
    • Waschuk, S.A.1    Bezerra, J.A.G.2    Shi, L.3    Brown, L.S.4
  • 17
    • 0021143119 scopus 로고
    • A rhodopsin is the functional photoreceptor for phototaxis in the unicellular eucaryote Chlamydomonas
    • Foster K. W., Saranak L., Patel N., Zarilli G., Okabe M., Kline T. and Nakanishi K. (1984) A rhodopsin is the functional photoreceptor for phototaxis in the unicellular eucaryote Chlamydomonas. Nature 311, 756-759.
    • (1984) Nature , vol.311 , pp. 756-759
    • Foster, K.W.1    Saranak, L.2    Patel, N.3    Zarilli, G.4    Okabe, M.5    Kline, T.6    Nakanishi, K.7
  • 18
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii
    • Sineshchekov O. A., Jung K. H. and Spudich J. L. (2002) Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 99, 8689-8694.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1    Jung, K.H.2    Spudich, J.L.3
  • 20
    • 0017625361 scopus 로고
    • Photoinduced inhibition and stimulation of respiration in cells of Halobacterium halobium: Kinetics, action spectra, relation to photoinduction of ΔpH
    • Litvin F. F., Boichenko V. A., Balashov S. P. and Dubrovskii V. T. (1977) Photoinduced inhibition and stimulation of respiration in cells of Halobacterium halobium: kinetics, action spectra, relation to photoinduction of ΔpH. Biofizika 22, 1062-1071.
    • (1977) Biofizika , vol.22 , pp. 1062-1071
    • Litvin, F.F.1    Boichenko, V.A.2    Balashov, S.P.3    Dubrovskii, V.T.4
  • 22
    • 0026714325 scopus 로고
    • Unique biphasic band shape of the visible circular dichroism of bacteriorhodopsin in purple membrane - excitons, multiple transitions or protein heterogeneity
    • Cassim J. Y. (1992) Unique biphasic band shape of the visible circular dichroism of bacteriorhodopsin in purple membrane - excitons, multiple transitions or protein heterogeneity. Biophys. J. 63, 1432-1442.
    • (1992) Biophys. J , vol.63 , pp. 1432-1442
    • Cassim, J.Y.1
  • 23
    • 0000035284 scopus 로고
    • Is there an excitonic interaction or antenna system in bacteriorhodopsin?
    • El-Sayed M. A., Lin C. T. and Mason W. R. (1989) Is there an excitonic interaction or antenna system in bacteriorhodopsin? Proc. Natl. Acad. Sci. USA 86, 5376-5379.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5376-5379
    • El-Sayed, M.A.1    Lin, C.T.2    Mason, W.R.3
  • 24
    • 0022978238 scopus 로고
    • Does retinol serve a sensitizing function in insect photoreceptors?
    • Kirschfeld K. and Vogt K. (1986) Does retinol serve a sensitizing function in insect photoreceptors? Vision Res. 26, 1771-1777.
    • (1986) Vision Res , vol.26 , pp. 1771-1777
    • Kirschfeld, K.1    Vogt, K.2
  • 27
    • 0016842838 scopus 로고
    • Two photosystems controlling behavioral responses of Halobacterium halobium
    • Hildebrand E. and Dencher N. (1975) Two photosystems controlling behavioral responses of Halobacterium halobium. Nature 257, 46-48.
    • (1975) Nature , vol.257 , pp. 46-48
    • Hildebrand, E.1    Dencher, N.2
  • 28
    • 0025024705 scopus 로고
    • Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II)
    • Takahashi T., Yan B., Mazur P., Derguini F., Nakanishi K. and Spudich J. L. (1990) Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II). Biochemistry 29, 8467-8474.
    • (1990) Biochemistry , vol.29 , pp. 8467-8474
    • Takahashi, T.1    Yan, B.2    Mazur, P.3    Derguini, F.4    Nakanishi, K.5    Spudich, J.L.6
  • 29
    • 0031820941 scopus 로고    scopus 로고
    • The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II
    • Chizhov I., Schmies G., Seidel R., Sydor J. R., Lüttenberg B. and Engelhard M. (1998) The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II. Biophys. J. 75, 999-1009.
    • (1998) Biophys. J , vol.75 , pp. 999-1009
    • Chizhov, I.1    Schmies, G.2    Seidel, R.3    Sydor, J.R.4    Lüttenberg, B.5    Engelhard, M.6
  • 30
    • 0034047356 scopus 로고    scopus 로고
    • The M intermediate of Pharaonis phoborhodopsin is photoactive
    • Balashov S. P., Sumi M. and Kamo N. (2000) The M intermediate of Pharaonis phoborhodopsin is photoactive. Biophys. J. 78, 3150-3159.
    • (2000) Biophys. J , vol.78 , pp. 3150-3159
    • Balashov, S.P.1    Sumi, M.2    Kamo, N.3
  • 32
    • 0017890594 scopus 로고
    • Photoreceptor electric potential in the phototaxis of the alga Haematococcus pluvialis
    • Litvin F. F., Sineshchekov O. A. and Sineshchekov V. A. (1978) Photoreceptor electric potential in the phototaxis of the alga Haematococcus pluvialis. Nature 271, 476-478.
    • (1978) Nature , vol.271 , pp. 476-478
    • Litvin, F.F.1    Sineshchekov, O.A.2    Sineshchekov, V.A.3
  • 33
    • 0033042090 scopus 로고    scopus 로고
    • Rhodopsin-mediated photosensing in green flagellated algae
    • Sineshchekov O. A. and Govorunova E. G. (1999) Rhodopsin-mediated photosensing in green flagellated algae. Trends Plant Sci. 4, 58-63.
    • (1999) Trends Plant Sci , vol.4 , pp. 58-63
    • Sineshchekov, O.A.1    Govorunova, E.G.2
  • 34
    • 84889393168 scopus 로고    scopus 로고
    • Sensory rhodopsin signaling in green flagellate algae
    • Briggs W. R, Spudich J. L, eds, Wiley-VCH, Weinheim
    • Sineshchekov O. A. and Spudich J. L. (2005) Sensory rhodopsin signaling in green flagellate algae. In: Handbook of Photosensory Receptors, pp. 25-42, Briggs W. R., Spudich J. L. (eds.), Wiley-VCH, Weinheim.
    • (2005) Handbook of Photosensory Receptors , pp. 25-42
    • Sineshchekov, O.A.1    Spudich, J.L.2
  • 35
    • 0036200510 scopus 로고    scopus 로고
    • Salinibacter ruber gen. nov., sp. nov., a novel, extremely halophilic member of the Bacteria from saltern crystallizer ponds
    • Antón J., Oren A., Benlloch S., Rodríguez-Valera F., Amann R. and Rosselló-Mora R. (2002) Salinibacter ruber gen. nov., sp. nov., a novel, extremely halophilic member of the Bacteria from saltern crystallizer ponds. Int. J. Syst. Evol. Microbiol. 52, 485-491.
    • (2002) Int. J. Syst. Evol. Microbiol , vol.52 , pp. 485-491
    • Antón, J.1    Oren, A.2    Benlloch, S.3    Rodríguez-Valera, F.4    Amann, R.5    Rosselló-Mora, R.6
  • 38
    • 0034734260 scopus 로고    scopus 로고
    • Protonation reactions and their coupling in bacteriorhodopsin
    • Balashov S. P. (2000) Protonation reactions and their coupling in bacteriorhodopsin. Biochim. Biophys. Acta 1460, 75-94.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 75-94
    • Balashov, S.P.1
  • 40
    • 33846875191 scopus 로고    scopus 로고
    • Substitution of Pro206 and Ser86 residues in the retinal binding pocket of Anabena sensory rhodopsin is not sufficient for proton pumping function
    • Choi A. R., Kim S. Y., Yoon S. R., Bae K. and Jung K.-H. (2007) Substitution of Pro206 and Ser86 residues in the retinal binding pocket of Anabena sensory rhodopsin is not sufficient for proton pumping function. J. Microbiol. Biotechnol. 17, 138-145.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 138-145
    • Choi, A.R.1    Kim, S.Y.2    Yoon, S.R.3    Bae, K.4    Jung, K.-H.5
  • 42
    • 0036741272 scopus 로고    scopus 로고
    • New C-40-carotenoid acyl glycoside as principal carotenoid in Salinibacter ruber, an extremely halophilic eubacterium
    • Lutnaes B. F., Oren A. and Liaaen-Jensen S. (2002) New C-40-carotenoid acyl glycoside as principal carotenoid in Salinibacter ruber, an extremely halophilic eubacterium. J. Nat. Prod. 65, 1340-1343.
    • (2002) J. Nat. Prod , vol.65 , pp. 1340-1343
    • Lutnaes, B.F.1    Oren, A.2    Liaaen-Jensen, S.3
  • 45
    • 2342532914 scopus 로고    scopus 로고
    • Protein regulation of carotenoid binding: Gatekeeper and locking amino acid residues in reaction centers of Rhodobacter sphaeroides
    • Roszak A. W., McKendrick K., Gardiner A. T., Mitchell I. A., Isaacs N. W., Cogdell R. J., Hashimoto H. and Frank H. A. (2004) Protein regulation of carotenoid binding: gatekeeper and locking amino acid residues in reaction centers of Rhodobacter sphaeroides. Structure 122, 765-773.
    • (2004) Structure , vol.122 , pp. 765-773
    • Roszak, A.W.1    McKendrick, K.2    Gardiner, A.T.3    Mitchell, I.A.4    Isaacs, N.W.5    Cogdell, R.J.6    Hashimoto, H.7    Frank, H.A.8
  • 46
    • 0000157456 scopus 로고
    • The photochemistry and function of carotenoids in photosynthesis
    • Young, A. and Britton, G, eds, Chapman and Hall, London
    • Frank H. A. and Cogdell R. J. (1993) The photochemistry and function of carotenoids in photosynthesis. In: Carotenoids in Photosynthesis, pp. 252-326, Young, A. and Britton, G. (eds.), Chapman and Hall, London.
    • (1993) Carotenoids in Photosynthesis , pp. 252-326
    • Frank, H.A.1    Cogdell, R.J.2
  • 47
    • 2342539764 scopus 로고    scopus 로고
    • Ultrafast dynamics of carotenoid excited states - from solution to natural and artificial systems
    • Polivka T. and Sundström V. (2004) Ultrafast dynamics of carotenoid excited states - from solution to natural and artificial systems. Chem. Rev. 104, 2021-2071.
    • (2004) Chem. Rev , vol.104 , pp. 2021-2071
    • Polivka, T.1    Sundström, V.2
  • 49
    • 0008652862 scopus 로고    scopus 로고
    • Dundas I. D. and Larsen H. (1962)The physiological role of the carotenoid pigments of Halobacterium salinarum. Arch. Mikrobiol. 44, 233-239.
    • Dundas I. D. and Larsen H. (1962)The physiological role of the carotenoid pigments of Halobacterium salinarum. Arch. Mikrobiol. 44, 233-239.
  • 50
    • 0018629255 scopus 로고
    • Photosensitization and quenching of singlet oxygen by pigments and lipids of photoreceptor cells of the retina
    • Krasnovsky A. A. Jr. and Kagan V. E. (1979) Photosensitization and quenching of singlet oxygen by pigments and lipids of photoreceptor cells of the retina. FEBS Lett. 108, 152-154.
    • (1979) FEBS Lett , vol.108 , pp. 152-154
    • Krasnovsky Jr., A.A.1    Kagan, V.E.2
  • 52
    • 34548645818 scopus 로고    scopus 로고
    • Goodwin T. W. (1980) The Biochemistry of the Carotenoids, 1, Plants, Chapman & Hall, London.
    • Goodwin T. W. (1980) The Biochemistry of the Carotenoids, vol 1, Plants, Chapman & Hall, London.
  • 53
    • 0000402734 scopus 로고    scopus 로고
    • The electronic states of carotenoids
    • Frank H. A, Young A. J, Britton G. and Cogdell R. J, eds, Kluwer Academic Publishers, Dordrecht
    • Christensen R. L. (1999) The electronic states of carotenoids. In: The Photochemistry of Carotenoids, pp. 137-157, Frank H. A., Young A. J., Britton G. and Cogdell R. J. (eds.), Kluwer Academic Publishers, Dordrecht.
    • (1999) The Photochemistry of Carotenoids , pp. 137-157
    • Christensen, R.L.1
  • 54
    • 34250965243 scopus 로고
    • Energiewanderung und Fluoreszenz
    • Förster T. (1946) Energiewanderung und Fluoreszenz. Naturwissenschaften 6, 166-175.
    • (1946) Naturwissenschaften , vol.6 , pp. 166-175
    • Förster, T.1
  • 56
    • 0033534585 scopus 로고    scopus 로고
    • Evolution of the archaeal rhodopsins: Evolution rate changes by gene duplication and functional differentiation
    • Ihara K., Umemura T., Katagiri I., Kitajima-Ihara T., Sugiyama Y., Kimura Y. and Mukohata Y. (1999) Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation. J. Mol. Biol. 285, 163-174.
    • (1999) J. Mol. Biol , vol.285 , pp. 163-174
    • Ihara, K.1    Umemura, T.2    Katagiri, I.3    Kitajima-Ihara, T.4    Sugiyama, Y.5    Kimura, Y.6    Mukohata, Y.7
  • 57
    • 1842531691 scopus 로고    scopus 로고
    • New insights into the evolution history of type 1 rhodopsins
    • Ruiz-Gonzales M. X. and Marin I. (2004) New insights into the evolution history of type 1 rhodopsins. J. Mol. Evol. 58, 348-358.
    • (2004) J. Mol. Evol , vol.58 , pp. 348-358
    • Ruiz-Gonzales, M.X.1    Marin, I.2
  • 58
    • 33749557420 scopus 로고    scopus 로고
    • Microbial rhodopsins: Functional versatility and genetic mobility
    • Sharma A. K., Spudich J. L. and Doolitle W. F. (2006) Microbial rhodopsins: functional versatility and genetic mobility. Trends Microbiol. 14, 463-469.
    • (2006) Trends Microbiol , vol.14 , pp. 463-469
    • Sharma, A.K.1    Spudich, J.L.2    Doolitle, W.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.