메뉴 건너뛰기




Volumn 587, Issue 15, 2013, Pages 2340-2345

Enzymatic characterization of an active NDH complex from thermosynechococcus elongatus

Author keywords

Cyanobacteria; Ferredoxin; Ferredoxin NADP + oxidoreductase; NADPH oxidation; NDH complex; Rotenone

Indexed keywords

FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; ISOENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ROTENONE;

EID: 84880697838     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.05.040     Document Type: Article
Times cited : (17)

References (44)
  • 1
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex i of bacteria and mitochondria and its homologue in chloroplasts
    • T. Friedrich, K. Steinmuller, and H. Weiss The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts FEBS Lett. 367 1995 107 111
    • (1995) FEBS Lett. , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmuller, K.2    Weiss, H.3
  • 2
    • 0001254606 scopus 로고
    • Donation of electrons from cytosolic components to the intersystem chain in the Cyanobacterium Synechococcus sp PCC-7002 as determined by the reduction of P700+
    • H.L. Mi, T. Endo, U. Schreiber, and K. Asada Donation of electrons from cytosolic components to the intersystem chain in the Cyanobacterium Synechococcus sp PCC-7002 as determined by the reduction of P700+ Plant Cell Physiol. 33 1992 1099 1105
    • (1992) Plant Cell Physiol. , vol.33 , pp. 1099-1105
    • Mi, H.L.1    Endo, T.2    Schreiber, U.3    Asada, K.4
  • 3
    • 0025845648 scopus 로고
    • A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC6803
    • T. Ogawa A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC6803 Proc. Natl. Acad. Sci. USA 88 1991 4275 4279
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4275-4279
    • Ogawa, T.1
  • 4
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex i of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • T. Friedrich, and D. Scheide The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases FEBS Lett. 479 2000 1 5
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 5
  • 6
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound, nadph-specific pyridine-nucleotide dehydrogenase complex mediates cyclic electron-transport in the cyanobacterium Synechocystis sp. PCC-6803
    • H.L. Mi, T. Endo, T. Ogawa, and K. Asada Thylakoid membrane-bound, nadph-specific pyridine-nucleotide dehydrogenase complex mediates cyclic electron-transport in the cyanobacterium Synechocystis sp. PCC-6803 Plant Cell Physiol. 36 1995 661 668
    • (1995) Plant Cell Physiol. , vol.36 , pp. 661-668
    • Mi, H.L.1    Endo, T.2    Ogawa, T.3    Asada, K.4
  • 7
    • 0028121693 scopus 로고
    • NAD(P)H dehydrogenase-dependent cyclic electron flow around photosystem-i in the cyanobacterium Synechocystis PCC-6803 - A study of dark-starved cells and spheroplasts
    • H. Mi, T. Endo, U. Schreiber, T. Ogawa, and K. Asada NAD(P)H dehydrogenase-dependent cyclic electron flow around photosystem-i in the cyanobacterium Synechocystis PCC-6803 - a study of dark-starved cells and spheroplasts Plant Cell Physiol. 35 1994 163 173
    • (1994) Plant Cell Physiol. , vol.35 , pp. 163-173
    • Mi, H.1    Endo, T.2    Schreiber, U.3    Ogawa, T.4    Asada, K.5
  • 8
    • 0035720458 scopus 로고    scopus 로고
    • Photo-induction of an NADPH dehydrogenase which functions as a mediator of electron transport to the intersystem chain in the cyanobacterium Synechocystis PCC6803
    • H.L. Mi, Y. Deng, Y. Tanaka, T. Hibino, and T. Takabe Photo-induction of an NADPH dehydrogenase which functions as a mediator of electron transport to the intersystem chain in the cyanobacterium Synechocystis PCC6803 Photosynth. Res. 70 2001 167 173
    • (2001) Photosynth. Res. , vol.70 , pp. 167-173
    • Mi, H.L.1    Deng, Y.2    Tanaka, Y.3    Hibino, T.4    Takabe, T.5
  • 9
    • 0038347204 scopus 로고    scopus 로고
    • 2 on NAD(P)H dehydrogenase, a mediator of cyclic electron transport around photosystem i in the cyanobacterium Synechocystis PCC6803
    • 2 on NAD(P)H dehydrogenase, a mediator of cyclic electron transport around photosystem I in the cyanobacterium Synechocystis PCC6803 Plant Cell Physiol. 44 2003 534 540
    • (2003) Plant Cell Physiol. , vol.44 , pp. 534-540
    • Deng, Y.1    Ye, J.Y.2    Mi, H.L.3
  • 10
    • 33750603691 scopus 로고    scopus 로고
    • Active NDH-1 complexes from the cyanobacterium Synechocystis sp. strain PCC 6803
    • W. Ma, Y. Deng, T. Ogawa, and H. Mi Active NDH-1 complexes from the cyanobacterium Synechocystis sp. strain PCC 6803 Plant Cell Physiol. 47 2006 1432 1436
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1432-1436
    • Ma, W.1    Deng, Y.2    Ogawa, T.3    Mi, H.4
  • 11
    • 38049181590 scopus 로고    scopus 로고
    • Redox of plastoquinone pool regulates the expression and activity of NADPH dehydrogenase supercomplex in Synechocystis sp. strain PCC 6803
    • W. Ma, Y. Deng, and H. Mi Redox of plastoquinone pool regulates the expression and activity of NADPH dehydrogenase supercomplex in Synechocystis sp. strain PCC 6803 Curr. Microbiol. 56 2008 189 193
    • (2008) Curr. Microbiol. , vol.56 , pp. 189-193
    • Ma, W.1    Deng, Y.2    Mi, H.3
  • 12
    • 0027191417 scopus 로고
    • Immunopurification of a subcomplex of the nad(p)h-plastoquinone- oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803
    • S. Berger, U. Ellersiek, D. Kinzelt, and K. Steinmuller Immunopurification of a subcomplex of the nad(p)h-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803 FEBS Lett. 326 1993 246 250
    • (1993) FEBS Lett. , vol.326 , pp. 246-250
    • Berger, S.1    Ellersiek, U.2    Kinzelt, D.3    Steinmuller, K.4
  • 13
    • 0032033348 scopus 로고    scopus 로고
    • Properties of the respiratory NAD(P)H dehydrogenase isolated from the cyanobacterium Synechocystis PCC6803
    • M. Matsuo, T. Endo, and K. Asada Properties of the respiratory NAD(P)H dehydrogenase isolated from the cyanobacterium Synechocystis PCC6803 Plant Cell Physiol. 39 1998 263 267
    • (1998) Plant Cell Physiol. , vol.39 , pp. 263-267
    • Matsuo, M.1    Endo, T.2    Asada, K.3
  • 14
    • 0141605899 scopus 로고    scopus 로고
    • Separation of hydrophobic NAD(P)H dehydrogenase subcomplexes from cyanobacterium Synechocystis PCC6803
    • Y. Deng, J.Y. Ye, H.L. Mi, and Y.G. Shen Separation of hydrophobic NAD(P)H dehydrogenase subcomplexes from cyanobacterium Synechocystis PCC6803 Acta Biochim. Biophys. Sin. 35 2003 723 727
    • (2003) Acta Biochim. Biophys. Sin. , vol.35 , pp. 723-727
    • Deng, Y.1    Ye, J.Y.2    Mi, H.L.3    Shen, Y.G.4
  • 15
    • 3142653751 scopus 로고    scopus 로고
    • Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803 - Identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex
    • P. Prommeenate, A.M. Lennon, C. Markert, M. Hippler, and P.J. Nixon Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803 - identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex J. Biol. Chem. 279 2004 28165 28173
    • (2004) J. Biol. Chem. , vol.279 , pp. 28165-28173
    • Prommeenate, P.1    Lennon, A.M.2    Markert, C.3    Hippler, M.4    Nixon, P.J.5
  • 16
    • 25144481313 scopus 로고    scopus 로고
    • Isolation, subunit composition and interaction of the NDH-1 complexes from Thermosynechococcus elongatus BP-1
    • P.P. Zhang Isolation, subunit composition and interaction of the NDH-1 complexes from Thermosynechococcus elongatus BP-1 Biochem. J. 390 2005 513 520
    • (2005) Biochem. J. , vol.390 , pp. 513-520
    • Zhang, P.P.1
  • 18
    • 79957773110 scopus 로고    scopus 로고
    • An Src homology 3 domain-like fold protein forms a ferredoxin binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis
    • H. Yamamoto, L. Peng, Y. Fukao, and T. Shikanai An Src homology 3 domain-like fold protein forms a ferredoxin binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis Plant Cell 23 2011 1480 1493
    • (2011) Plant Cell , vol.23 , pp. 1480-1493
    • Yamamoto, H.1    Peng, L.2    Fukao, Y.3    Shikanai, T.4
  • 19
    • 84858055706 scopus 로고    scopus 로고
    • Identification of novel Ssl0352 protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH: Plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803
    • N. Battchikova, L. Wei, L. Du, L. Bersanini, E.-M. Aro, and W. Ma Identification of novel Ssl0352 protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH: plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803 J. Biol. Chem. 287 2012 8660
    • (2012) J. Biol. Chem. , vol.287 , pp. 8660
    • Battchikova, N.1    Wei, L.2    Du, L.3    Bersanini, L.4    Aro, E.-M.5    Ma, W.6
  • 20
    • 84984087585 scopus 로고
    • Simple conditions for growth of unicellular blue-green algae on plates
    • M.M. Allen Simple conditions for growth of unicellular blue-green algae on plates J. Phycol. 4 1968 1-4
    • (1968) J. Phycol. , vol.4 , pp. 1-4
    • Allen, M.M.1
  • 21
    • 0028606359 scopus 로고
    • The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane-lipids - A mechanism of chilling tolerance
    • Z. Gombos, H. Wada, and N. Murata The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane-lipids - a mechanism of chilling tolerance Proc. Natl. Acad. Sci. USA 91 1994 8787 8791
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8787-8791
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 22
    • 78651153791 scopus 로고
    • Disc electrophoresis: 2. Method and application to human serum proteins
    • B.J. Davis Disc electrophoresis: 2. Method and application to human serum proteins Ann. NY Acad. Sci. 121 1964 404-427
    • (1964) Ann. NY Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0018400873 scopus 로고
    • Mitochondrial electron-transport inhibitors
    • T.P. Singer Mitochondrial electron-transport inhibitors Methods Enzymol. 55 1979 454 462
    • (1979) Methods Enzymol. , vol.55 , pp. 454-462
    • Singer, T.P.1
  • 26
    • 18844436373 scopus 로고    scopus 로고
    • Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp. PCC 6803
    • P.P. Zhang, N. Battchikova, T. Jansen, J. Appel, T. Ogawa, and E.M. Aro Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp. PCC 6803 Plant Cell 16 2004 3326 3340
    • (2004) Plant Cell , vol.16 , pp. 3326-3340
    • Zhang, P.P.1    Battchikova, N.2    Jansen, T.3    Appel, J.4    Ogawa, T.5    Aro, E.M.6
  • 27
    • 13244281728 scopus 로고    scopus 로고
    • Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803
    • N. Battchikova, P. Zhang, S. Rudd, T. Ogawa, and E.M. Aro Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803 J. Biol. Chem. 280 2005 2587 2595
    • (2005) J. Biol. Chem. , vol.280 , pp. 2587-2595
    • Battchikova, N.1    Zhang, P.2    Rudd, S.3    Ogawa, T.4    Aro, E.M.5
  • 28
  • 29
    • 0030043480 scopus 로고    scopus 로고
    • Evidence for an association of ndh B, ndh J gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex
    • G. Guedeney, S. Corneille, S. Cuine, and G. Peltier Evidence For an association of ndh B, ndh J gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex FEBS Lett. 378 1996 277 280
    • (1996) FEBS Lett. , vol.378 , pp. 277-280
    • Guedeney, G.1    Corneille, S.2    Cuine, S.3    Peltier, G.4
  • 30
    • 0027235331 scopus 로고
    • Binding of ferredoxin to ferredoxin-NADP+ oxidoreductase - The role of carboxyl groups, electrostatic surface-potential, and molecular dipole-moment
    • A.R. Depascalis, I. Jelesarov, F. Ackermann, W.H. Koppenol, M. Hirasawa, D.B. Knaff, and H.R. Bosshard Binding of ferredoxin to ferredoxin-NADP+ oxidoreductase - the role of carboxyl groups, electrostatic surface-potential, and molecular dipole-moment Protein Sci. 2 1993 1126 1135
    • (1993) Protein Sci. , vol.2 , pp. 1126-1135
    • Depascalis, A.R.1    Jelesarov, I.2    Ackermann, F.3    Koppenol, W.H.4    Hirasawa, M.5    Knaff, D.B.6    Bosshard, H.R.7
  • 31
    • 0027033884 scopus 로고
    • Cloning and transcription analysis of the ndh(A-I-G-E) gene-cluster and the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803
    • U. Ellersiek, and K. Steinmuller Cloning and transcription analysis of the ndh(A-I-G-E) gene-cluster and the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803 Plant Mol. Biol. 20 1992 1097 1110
    • (1992) Plant Mol. Biol. , vol.20 , pp. 1097-1110
    • Ellersiek, U.1    Steinmuller, K.2
  • 33
    • 0014646190 scopus 로고
    • Fluorescence and oxygen evolution from chlorella pyrenoidosa
    • C. Bonavent, and J. Myers Fluorescence and oxygen evolution from chlorella pyrenoidosa Biochim. Biophys. Acta 189 1969 189-366
    • (1969) Biochim. Biophys. Acta , vol.189 , pp. 189-366
    • Bonavent, C.1    Myers, J.2
  • 34
    • 0014686888 scopus 로고
    • Control of excitation transfer in photosynthesis 2. Magnesium ion-dependent distribution of excitation energy between 2 pigment systems in spinach chloroplasts
    • N. Murata Control of excitation transfer in photosynthesis 2. Magnesium ion-dependent distribution of excitation energy between 2 pigment systems in spinach chloroplasts Biochim. Biophys. Acta 189 1969 171-181
    • (1969) Biochim. Biophys. Acta , vol.189 , pp. 171-181
    • Murata, N.1
  • 35
    • 0022338638 scopus 로고
    • Correlation of membrane-protein phosphorylation with excitation-energy distribution in the cyanobacterium synechococcus-6301
    • J.F. Allen, C.E. Sanders, and N.G. Holmes Correlation of membrane-protein phosphorylation with excitation-energy distribution in the cyanobacterium synechococcus-6301 FEBS Lett. 193 1985 271 275
    • (1985) FEBS Lett. , vol.193 , pp. 271-275
    • Allen, J.F.1    Sanders, C.E.2    Holmes, N.G.3
  • 36
    • 0344716850 scopus 로고
    • P-700 photooxidation in state-1 and state-2 in cyanobacteria upon flash illumination with phycobilin-absorbed and chlorophyll-absorbed light
    • N.F. Tsinoremas, J.A.M. Hubbard, M.C.W. Evans, and J.F. Allen P-700 photooxidation in state-1 and state-2 in cyanobacteria upon flash illumination with phycobilin-absorbed and chlorophyll-absorbed light FEBS Lett. 256 1989 106 110
    • (1989) FEBS Lett. , vol.256 , pp. 106-110
    • Tsinoremas, N.F.1    Hubbard, J.A.M.2    Evans, M.C.W.3    Allen, J.F.4
  • 37
    • 0026556851 scopus 로고
    • Protein-phosphorylation in regulation of photosynthesis
    • J.F. Allen Protein-phosphorylation in regulation of photosynthesis Biochim. Biophys. Acta 1098 1992 275 335
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 38
    • 4444305451 scopus 로고    scopus 로고
    • Phycobilisome diffusion is required for light-state transitions in cyanobacterial
    • S. Joshua, and C.W. Mullineaux Phycobilisome diffusion is required for light-state transitions in cyanobacterial Plant Physiol. 135 2004 2112 2119
    • (2004) Plant Physiol. , vol.135 , pp. 2112-2119
    • Joshua, S.1    Mullineaux, C.W.2
  • 39
    • 36849039532 scopus 로고    scopus 로고
    • Estimation of relative contribution of "mobile phycobilisome" and "energy spillover" in the light-dark induced state transition in Spirulina platensis
    • R. Zhang, H. Li, J. Xie, and J.Q. Zhao Estimation of relative contribution of "mobile phycobilisome" and "energy spillover" in the light-dark induced state transition in Spirulina platensis Photosynth. Res. 94 2007 315 320
    • (2007) Photosynth. Res. , vol.94 , pp. 315-320
    • Zhang, R.1    Li, H.2    Xie, J.3    Zhao, J.Q.4
  • 40
    • 0036851204 scopus 로고    scopus 로고
    • Regulation of the distribution of chlorophyll and phycobilin-absorbed excitation energy in cyanobacteria. A structure-based model for the light state transition
    • M.D. McConnell, R. Koop, S. Vasil'ev, and D. Bruce Regulation of the distribution of chlorophyll and phycobilin-absorbed excitation energy in cyanobacteria. A structure-based model for the light state transition Plant Physiol. 130 2002 1201 1212
    • (2002) Plant Physiol. , vol.130 , pp. 1201-1212
    • McConnell, M.D.1    Koop, R.2    Vasil'Ev, S.3    Bruce, D.4
  • 41
    • 33750580424 scopus 로고    scopus 로고
    • The state transition mechanism - Simply depending on light-on and -off in Spirulina platensis
    • H. Li, D.H. Li, S.Z. Yang, H. Xie, and J.Q. Zhao The state transition mechanism - simply depending on light-on and -off in Spirulina platensis Biochim. Biophys. Acta Bioenerg. 1757 2006 1512 1519
    • (2006) Biochim. Biophys. Acta Bioenerg. , vol.1757 , pp. 1512-1519
    • Li, H.1    Li, D.H.2    Yang, S.Z.3    Xie, H.4    Zhao, J.Q.5
  • 42
    • 34249875177 scopus 로고    scopus 로고
    • Changes in cyclic and respiratory electron transport by the movement of phycobilisomes in the cyanobacterium Synechocystis sp. strain PCC 6803
    • W.M. Ma, T. Ogawa, Y.G. Shen, and H.L. Mi Changes in cyclic and respiratory electron transport by the movement of phycobilisomes in the cyanobacterium Synechocystis sp. strain PCC 6803 Biochim. Biophys. Acta Bioenerg. 1767 2007 742 749
    • (2007) Biochim. Biophys. Acta Bioenerg. , vol.1767 , pp. 742-749
    • Ma, W.M.1    Ogawa, T.2    Shen, Y.G.3    Mi, H.L.4
  • 43
    • 0028830806 scopus 로고
    • Quenching analysis of chlorophyll fluorescence by the saturation pulse method - Particular aspects relating to the study of eukaryotic algae and cyanobacteria
    • U. Schreiber, T. Endo, H.L. Mi, and K. Asada Quenching analysis of chlorophyll fluorescence by the saturation pulse method - particular aspects relating to the study of eukaryotic algae and cyanobacteria Plant Cell Physiol. 36 1995 873 882
    • (1995) Plant Cell Physiol. , vol.36 , pp. 873-882
    • Schreiber, U.1    Endo, T.2    Mi, H.L.3    Asada, K.4
  • 44
    • 0033517096 scopus 로고    scopus 로고
    • Localization and function of ferredoxin: NADP(+) reductase bound to the phycobilisomes of Synechocystis
    • J.J. van Thor, O.W.M. Gruters, H.C.P. Matthijs, and K.J. Hellingwerf Localization and function of ferredoxin: NADP(+) reductase bound to the phycobilisomes of Synechocystis EMBO J. 18 1999 4128 4136
    • (1999) EMBO J. , vol.18 , pp. 4128-4136
    • Van Thor, J.J.1    Gruters, O.W.M.2    Matthijs, H.C.P.3    Hellingwerf, K.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.