메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Real-time kinetics of electrogenic Na+ transport by rhodopsin from the marine flavobacterium Dokdonia sp. PRO95

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MONOVALENT CATION; PROTEIN BINDING; PROTEOLIPID; PROTEOLIPOSOMES; RECOMBINANT PROTEIN; RHODOPSIN; SODIUM;

EID: 84958559549     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep21397     Document Type: Article
Times cited : (28)

References (41)
  • 1
    • 84892159791 scopus 로고    scopus 로고
    • Microbial and animal rhodopsins: Structures, functions, and molecular mechanisms
    • Ernst, O. P. et al. Microbial and animal rhodopsins: structures, functions, and molecular mechanisms. Chem. Rev. 114, 126-163 (2014).
    • (2014) Chem. Rev. , vol.114 , pp. 126-163
    • Ernst, O.P.1
  • 3
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D. & Stoeckenius, W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat. New Biol. 233, 149-152 (1971).
    • (1971) Nat. New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 4
    • 84897114580 scopus 로고    scopus 로고
    • Of ion pumps, sensors and channels-perspectives on microbial rhodopsins between science and history
    • Grote, M., Engelhard, M. & Hegemann, P. Of ion pumps, sensors and channels-perspectives on microbial rhodopsins between science and history. Biochim. Biophys. Acta 1837, 533-545 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 533-545
    • Grote, M.1    Engelhard, M.2    Hegemann, P.3
  • 5
    • 84877767837 scopus 로고    scopus 로고
    • A light-driven sodium ion pump in marine bacteria
    • Inoue, K. et al. A light-driven sodium ion pump in marine bacteria. Nat. Commun. 4, 1678 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1678
    • Inoue, K.1
  • 7
    • 84899850284 scopus 로고    scopus 로고
    • Functional characterization of flavobacteria rhodopsins reveals a unique class of light-driven chloride pump in bacteria
    • Yoshizawa, S. et al. Functional characterization of flavobacteria rhodopsins reveals a unique class of light-driven chloride pump in bacteria. Proc. Natl. Acad. Sci. USA 111, 6732-6737 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 6732-6737
    • Yoshizawa, S.1
  • 8
    • 84916620044 scopus 로고    scopus 로고
    • + binding site is formed transiently in the photocycle
    • + binding site is formed transiently in the photocycle. Biochemistry 53, 7549-7561 (2014).
    • (2014) Biochemistry , vol.53 , pp. 7549-7561
    • Balashov, S.P.1
  • 10
    • 84876527252 scopus 로고    scopus 로고
    • Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana) dokdonensis and identification of a novel class of rhodopsins
    • Kwon, S. K. et al. Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana) dokdonensis and identification of a novel class of rhodopsins. Genome Biol. Evol. 5, 187-199 (2013).
    • (2013) Genome Biol. Evol. , vol.5 , pp. 187-199
    • Kwon, S.K.1
  • 11
    • 84929173717 scopus 로고    scopus 로고
    • Crystal structure of a light-driven sodium pump
    • Gushchin, I. et al. Crystal structure of a light-driven sodium pump. Nat. Struct. Mol. Biol. 22, 390-395 (2015).
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 390-395
    • Gushchin, I.1
  • 12
    • 84929095986 scopus 로고    scopus 로고
    • + pump
    • + pump. Nature 521, 48-53 (2015).
    • (2015) Nature , vol.521 , pp. 48-53
    • Kato, H.E.1
  • 13
    • 0022616887 scopus 로고
    • The effect of cytochrome c, hexammineruthenium and ubiquinone-10 on the kinetics of photoelectric responses of Rhodospirillum rubrum reaction centres
    • Drachev, L. A. et al. The effect of cytochrome c, hexammineruthenium and ubiquinone-10 on the kinetics of photoelectric responses of Rhodospirillum rubrum reaction centres. Biochim. Biophys. Acta 848, 137-146 (1986).
    • (1986) Biochim. Biophys. Acta , vol.848 , pp. 137-146
    • Drachev, L.A.1
  • 14
    • 0024286692 scopus 로고
    • Electrogenic steps in the redox reactions catalyzed by photosynthetic reaction-centre complex from Rhodopseudomonas viridis
    • Dracheva, S. M. et al. Electrogenic steps in the redox reactions catalyzed by photosynthetic reaction-centre complex from Rhodopseudomonas viridis. Eur. J. Bioehem. 171, 253-264 (1988).
    • (1988) Eur. J. Bioehem. , vol.171 , pp. 253-264
    • Dracheva, S.M.1
  • 15
    • 0000056451 scopus 로고
    • 1 complexes of Rhodobacter sphaeroides chromatophores
    • 1 complexes of Rhodobacter sphaeroides chromatophores. Biochim. Biophys. Acta 973, 189-197 (1989).
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 189-197
    • Drachev, L.A.1
  • 17
    • 57849107989 scopus 로고    scopus 로고
    • Electrogenic reactions and dielectric properties of photosystem II
    • Semenov, A., Cherepanov, D. & Mamedov, M. Electrogenic reactions and dielectric properties of photosystem II. Photosynth. Res. 98, 121-130 (2008).
    • (2008) Photosynth. Res. , vol.98 , pp. 121-130
    • Semenov, A.1    Cherepanov, D.2    Mamedov, M.3
  • 19
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • Konstantinov, A. A., Siletsky, S., Mitchell, D., Kaulen, A. & Gennis, R. B. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. Proc. Natl. Acad. Sci. USA 94, 9085-9090 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 20
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • Jasaitis, A., Verkhovsky, M. I., Morgan, J. E., Verkhovskaya, M. L. & Wikström, M. Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen. Biochemistry 38, 2697-2706 (1999).
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikström, M.5
  • 21
    • 14844351539 scopus 로고    scopus 로고
    • Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site
    • Belevich, I. et al. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proc. Natl. Acad. Sci. USA 102, 3657-3662 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3657-3662
    • Belevich, I.1
  • 22
    • 0016313475 scopus 로고
    • +-ATPase and bacteriorhodopsin
    • +-ATPase and bacteriorhodopsin. Nature 249, 321-324 (1974).
    • (1974) Nature , vol.249 , pp. 321-324
    • Drachev, L.A.1
  • 23
    • 0034734240 scopus 로고    scopus 로고
    • Electrogenic processes and protein conformational changes accompanying the bacteriorhodopsin photocycle
    • Kaulen, A. D. Electrogenic processes and protein conformational changes accompanying the bacteriorhodopsin photocycle. Biochim. Biophys. Acta 1460, 204-219 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 204-219
    • Kaulen, A.D.1
  • 24
    • 0032079347 scopus 로고    scopus 로고
    • Flash-induced voltage changes in halorhodopsin from Natronobacterium pharaonis
    • Kalaidzidis, I. V., Kalaidzidis, Y. L. & Kaulen, A. D. Flash-induced voltage changes in halorhodopsin from Natronobacterium pharaonis. FEBS Lett. 427, 59-63 (1998).
    • (1998) FEBS Lett. , vol.427 , pp. 59-63
    • Kalaidzidis, I.V.1    Kalaidzidis, Y.L.2    Kaulen, A.D.3
  • 25
    • 84921783015 scopus 로고    scopus 로고
    • Electrogenic and nonelectrogenic ion fluxes across lipid and mitochondrial membranes mediated by monensin and monensin ethyl ester
    • Antonenko, Y. N., Rokitskaya, T. I. & Huczyński, A. Electrogenic and nonelectrogenic ion fluxes across lipid and mitochondrial membranes mediated by monensin and monensin ethyl ester. Biochim Biophys Acta 1848, 995-1004 (2015).
    • (2015) Biochim Biophys Acta , vol.1848 , pp. 995-1004
    • Antonenko, Y.N.1    Rokitskaya, T.I.2    Huczyński, A.3
  • 26
    • 0017709781 scopus 로고
    • Sodium complexation by the calcium binding site of parvalbumin
    • Grandjean, J., Laszlo, P. & Gerday, C. Sodium complexation by the calcium binding site of parvalbumin. FEBS Lett. 81, 376-380 (1977).
    • (1977) FEBS Lett. , vol.81 , pp. 376-380
    • Grandjean, J.1    Laszlo, P.2    Gerday, C.3
  • 27
    • 0022375963 scopus 로고
    • 23Na ions interacting with the gramicidin channel
    • 23Na ions interacting with the gramicidin channel. Biophys. J. 48, 643-662 (1985).
    • (1985) Biophys. J. , vol.48 , pp. 643-662
    • Monoi, H.1
  • 29
    • 84933556149 scopus 로고    scopus 로고
    • Cation-specific conformations in a dual-function ion-pumping microbial rhodopsin
    • da Silva, G. F., Goblirsch, B. R., Tsai, A. L. & Spudich, J. L. Cation-specific conformations in a dual-function ion-pumping microbial rhodopsin. Biochemistry 54, 3950-3959 (2015).
    • (2015) Biochemistry , vol.54 , pp. 3950-3959
    • Da Silva, G.F.1    Goblirsch, B.R.2    Tsai, A.L.3    Spudich, J.L.4
  • 30
    • 84944872760 scopus 로고    scopus 로고
    • Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins
    • Shalaeva, D. N., Galperin, M. Y. & Mulkidjanian, A. Y. Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins. Biol. Direct 10, 63 (2015).
    • (2015) Biol. Direct , vol.10 , pp. 63
    • Shalaeva, D.N.1    Galperin, M.Y.2    Mulkidjanian, A.Y.3
  • 33
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144-148 (1961).
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 34
    • 46349090280 scopus 로고    scopus 로고
    • The past and present of the sodium energetics: May the sodium-motive force be with you
    • Mulkidjanian, A. Y., Dibrov, P. & Galperin, M. Y. The past and present of the sodium energetics: May the sodium-motive force be with you, Biochim. Biophys. Acta 1777, 985-992 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 985-992
    • Mulkidjanian, A.Y.1    Dibrov, P.2    Galperin, M.Y.3
  • 35
    • 0343558857 scopus 로고
    • A single turnover study of photoelectric current-generating proteins
    • Skulachev, V. P. A single turnover study of photoelectric current-generating proteins. Methods Enzymol. 88, 35-45 (1982).
    • (1982) Methods Enzymol. , vol.88 , pp. 35-45
    • Skulachev, V.P.1
  • 40
    • 65549108958 scopus 로고    scopus 로고
    • +-translocating NADH: Ubiquinone oxidoreductase catalytic cycle resolved by the ultrafast freeze-quench approach
    • +-translocating NADH: ubiquinone oxidoreductase catalytic cycle resolved by the ultrafast freeze-quench approach. J. Biol. Chem. 284, 5533-5538 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 5533-5538
    • Bogachev, A.V.1    Belevich, N.P.2    Bertsova, Y.V.3    Verkhovsky, M.I.4
  • 41
    • 0000336683 scopus 로고
    • Regularization techniques for inverse problems in molecular biology
    • P. Deuflhard & E. Hairer, (Eds.), Birkhauser, Boston
    • Provencher, S. W. & Vogel, R. H. Regularization techniques for inverse problems in molecular biology In P. Deuflhard & E. Hairer, (Eds.), Progress in scientific computing, Birkhauser, Boston, 2, pp. 304-319 (1983).
    • (1983) Progress in Scientific Computing , vol.2 , pp. 304-319
    • Provencher, S.W.1    Vogel, R.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.