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Volumn 96, Issue 3, 2009, Pages 201-206

Methylamine interaction with proteins of photosystem II: A comparison with biogenic polyamines

Author keywords

FTIR spectroscopy; Methylamine; Oxygen evolution; Photosystem II; Protein secondary structure

Indexed keywords

CHLOROPHYLL; METHYLAMINE; POLYPEPTIDE; PUTRESCINE; SPERMIDINE; SPERMINE;

EID: 68649103279     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2009.06.006     Document Type: Article
Times cited : (6)

References (38)
  • 4
    • 0000971931 scopus 로고
    • Polyamines in barley seedlings
    • Smith T.A., and Best G.R. Polyamines in barley seedlings. Phytochemistry 16 (1977) 841-843
    • (1977) Phytochemistry , vol.16 , pp. 841-843
    • Smith, T.A.1    Best, G.R.2
  • 5
    • 41449116568 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II
    • Sproviero E.M., Gascon J.A., McEvoy J.P., Brudvig G.W., and Batista V.S. Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II. J. Am. Chem. Soc. 130 (2008) 3428-3442
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3428-3442
    • Sproviero, E.M.1    Gascon, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 6
    • 0031023829 scopus 로고    scopus 로고
    • The effects of spermine and spermidine on the structure of photosystem II proteins in relation to inhibition of electron transport
    • Bograh A., Gingras Y., Tajmir-Riahi H.A., and Carpentier R. The effects of spermine and spermidine on the structure of photosystem II proteins in relation to inhibition of electron transport. FEBS Lett. 402 (1997) 41-44
    • (1997) FEBS Lett. , vol.402 , pp. 41-44
    • Bograh, A.1    Gingras, Y.2    Tajmir-Riahi, H.A.3    Carpentier, R.4
  • 7
    • 33947306395 scopus 로고    scopus 로고
    • Interaction of polyamines with proteins of photosystem II: cation binding and photosynthetic oxygen evolution
    • Beauchemin R., Harnois J., Rouillon R., Tajmir-Riahi H.A., and Carpentier R. Interaction of polyamines with proteins of photosystem II: cation binding and photosynthetic oxygen evolution. J. Mol. Struct. 833 (2007) 169-174
    • (2007) J. Mol. Struct. , vol.833 , pp. 169-174
    • Beauchemin, R.1    Harnois, J.2    Rouillon, R.3    Tajmir-Riahi, H.A.4    Carpentier, R.5
  • 8
    • 34447103566 scopus 로고    scopus 로고
    • Spermine and spermidine inhibition of photosystem II: disassembly of the oxygen evolving complex and consequent perturbation in electron donation from TyrZ to P680+ and the quinone acceptors QA- to QB
    • Beauchemin R., Gautier A., Harnois J., Boisvert S., Govidachary S., and Carpentier R. Spermine and spermidine inhibition of photosystem II: disassembly of the oxygen evolving complex and consequent perturbation in electron donation from TyrZ to P680+ and the quinone acceptors QA- to QB. Biochim. Biophys. Acta 1767 (2007) 905-912
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 905-912
    • Beauchemin, R.1    Gautier, A.2    Harnois, J.3    Boisvert, S.4    Govidachary, S.5    Carpentier, R.6
  • 9
    • 0028855124 scopus 로고
    • Effects of Sr-2+, Ca-2+, and spermine on thylakoid protein and chlorophyll degradation during dark incubation of sugar beet leaf discs
    • Kim T.W., and Heinrich G. Effects of Sr-2+, Ca-2+, and spermine on thylakoid protein and chlorophyll degradation during dark incubation of sugar beet leaf discs. Photosynthetica 31 (1995) 315-319
    • (1995) Photosynthetica , vol.31 , pp. 315-319
    • Kim, T.W.1    Heinrich, G.2
  • 10
    • 0029012387 scopus 로고
    • Influence of polyamine inhibitors on light-independent and light-dependent chlorophyll biosynthesis and on the photosynthetic rate
    • Beigbeder A., Vavadakis M., Navakoudis E., and Kotzabasis K. Influence of polyamine inhibitors on light-independent and light-dependent chlorophyll biosynthesis and on the photosynthetic rate. J. Photochem. Photobiol. B 28 (1995) 235-242
    • (1995) J. Photochem. Photobiol. B , vol.28 , pp. 235-242
    • Beigbeder, A.1    Vavadakis, M.2    Navakoudis, E.3    Kotzabasis, K.4
  • 11
    • 0003157614 scopus 로고
    • Effect of some polyamines on the functional activity of thylakoid membranes
    • Iordanov I.T., Goltsev V., Doltchinkova V., and Kruleva L. Effect of some polyamines on the functional activity of thylakoid membranes. Photosynthetica 23 (1989) 314-323
    • (1989) Photosynthetica , vol.23 , pp. 314-323
    • Iordanov, I.T.1    Goltsev, V.2    Doltchinkova, V.3    Kruleva, L.4
  • 12
    • 0028356315 scopus 로고
    • The influence of exogenously supplied spermine on protochlorophyllide and chlorophyll biosynthesis
    • Beigbeder A., and Kotzabasis K. The influence of exogenously supplied spermine on protochlorophyllide and chlorophyll biosynthesis. J. Photochem. Photobiol. B 23 (1994) 201-206
    • (1994) J. Photochem. Photobiol. B , vol.23 , pp. 201-206
    • Beigbeder, A.1    Kotzabasis, K.2
  • 13
    • 0030799356 scopus 로고    scopus 로고
    • Role of light in changes in free amino acid and polyamine contents at chilling temperature in maize
    • Szalai G., Janda T., Bartok T., and Paldi E. Role of light in changes in free amino acid and polyamine contents at chilling temperature in maize. Physiol. Plant 101 (1997) 434-438
    • (1997) Physiol. Plant , vol.101 , pp. 434-438
    • Szalai, G.1    Janda, T.2    Bartok, T.3    Paldi, E.4
  • 14
    • 0031789554 scopus 로고    scopus 로고
    • Differential changes in the photosynthetic pigments and polyamine content during photoadaptation and photoinhibition of the unicellular green alga Scenedesmus obliquus
    • Kotzabasis K., and Dörnemann D. Differential changes in the photosynthetic pigments and polyamine content during photoadaptation and photoinhibition of the unicellular green alga Scenedesmus obliquus. Z. Naturforsch 53c (1998) 833-840
    • (1998) Z. Naturforsch , vol.53 c , pp. 833-840
    • Kotzabasis, K.1    Dörnemann, D.2
  • 15
    • 0033133996 scopus 로고    scopus 로고
    • The regulatory role of polyamines in structure and functioning of the photosynthetic apparatus during photoadaptation
    • Kotzabasis K., Strasser B., Navakoudis E., Senger H., and Dörnemann D. The regulatory role of polyamines in structure and functioning of the photosynthetic apparatus during photoadaptation. J. Photochem. Photobiol. B 50 (1999) 45-52
    • (1999) J. Photochem. Photobiol. B , vol.50 , pp. 45-52
    • Kotzabasis, K.1    Strasser, B.2    Navakoudis, E.3    Senger, H.4    Dörnemann, D.5
  • 16
    • 0032811887 scopus 로고    scopus 로고
    • Role of spermidine in the stabilization of the apoprotein of the light-harvesting chlorophyll a/b-protein complex of photosystem II during leaf senescence process
    • Legocka J., and Zajchert I. Role of spermidine in the stabilization of the apoprotein of the light-harvesting chlorophyll a/b-protein complex of photosystem II during leaf senescence process. Acta Physiol. Plant 21 (1999) 127-132
    • (1999) Acta Physiol. Plant , vol.21 , pp. 127-132
    • Legocka, J.1    Zajchert, I.2
  • 17
    • 0002575553 scopus 로고
    • The chloride requirement for photosynthetic oxygen evolution: factors affecting nucleophilic displacement of chloride from the oxygen-evolving complex
    • Sandusky P.O., and Yocum C.F. The chloride requirement for photosynthetic oxygen evolution: factors affecting nucleophilic displacement of chloride from the oxygen-evolving complex. Biochim. Biophys. Acta 849 (1986) 85-93
    • (1986) Biochim. Biophys. Acta , vol.849 , pp. 85-93
    • Sandusky, P.O.1    Yocum, C.F.2
  • 18
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes EPR and electron-transport properties
    • Berthold D.A., Babcock G.T., and Yocum C.F. A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes EPR and electron-transport properties. FEBS Lett. 134 (1981) 231-234
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 19
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra R.J., Thompson W.A., and Kriedemann P.E. Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta 975 (1989) 384-394
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 20
    • 0033080488 scopus 로고    scopus 로고
    • The effect of cholesterol on the solution structure of proteins of photosystem II. Protein secondary structure and photosynthetic oxygen evolution
    • Bograh A., Carpentier R., and Tajmir-Riahi H.A. The effect of cholesterol on the solution structure of proteins of photosystem II. Protein secondary structure and photosynthetic oxygen evolution. J. Colloid Interface Sci. 210 (1999) 118-122
    • (1999) J. Colloid Interface Sci. , vol.210 , pp. 118-122
    • Bograh, A.1    Carpentier, R.2    Tajmir-Riahi, H.A.3
  • 21
    • 0028907510 scopus 로고
    • A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy
    • Ahmed A., Tajmir-Riahi H.A., and Carpentier R. A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy. FEBS Lett. 363 (1995) 65-68
    • (1995) FEBS Lett. , vol.363 , pp. 65-68
    • Ahmed, A.1    Tajmir-Riahi, H.A.2    Carpentier, R.3
  • 24
    • 0029787928 scopus 로고    scopus 로고
    • 2 assimilation rates and different kinds of chlorophyll fluorescence ratios
    • 2 assimilation rates and different kinds of chlorophyll fluorescence ratios. J. Plant Physiol. 148 (1996) 555-566
    • (1996) J. Plant Physiol. , vol.148 , pp. 555-566
    • Babani, F.1    Lichtenthaler, H.K.2
  • 25
    • 2942532508 scopus 로고    scopus 로고
    • Photosystem II inhibition by moderate light under low temperature in intact leaves of chilling-sensitive and tolerant plants
    • Govindachary S., Bukhov N., Joly D., and Carpentier R. Photosystem II inhibition by moderate light under low temperature in intact leaves of chilling-sensitive and tolerant plants. Physiol. Plant 121 (2004) 322-333
    • (2004) Physiol. Plant , vol.121 , pp. 322-333
    • Govindachary, S.1    Bukhov, N.2    Joly, D.3    Carpentier, R.4
  • 26
    • 30044440683 scopus 로고    scopus 로고
    • The polyphasic chlorophyll a fluorescence rise measured under high intensity of exciting light
    • Lazar D. The polyphasic chlorophyll a fluorescence rise measured under high intensity of exciting light. Funct. Plant Biol. 33 (2006) 9-30
    • (2006) Funct. Plant Biol. , vol.33 , pp. 9-30
    • Lazar, D.1
  • 27
    • 28444454056 scopus 로고    scopus 로고
    • Chlorophyll a fluorescence induction kinetics in leaves predicted from a model describing each discrete step of excitation energy and electron transfer associated with photosystem II
    • Zhu X.G., Govindjee, Baker N.R., Desturler E., Ort D.R., and Long S.P. Chlorophyll a fluorescence induction kinetics in leaves predicted from a model describing each discrete step of excitation energy and electron transfer associated with photosystem II. Planta 223 (2005) 114-133
    • (2005) Planta , vol.223 , pp. 114-133
    • Zhu, X.G.1    Govindjee2    Baker, N.R.3    Desturler, E.4    Ort, D.R.5    Long, S.P.6
  • 28
    • 0034464702 scopus 로고    scopus 로고
    • Chlorophyll fluorescence transients of photosystem II membrane particles as a tool for studying photosynthetic oxygen evolution
    • Pospíšil P., and Dau H. Chlorophyll fluorescence transients of photosystem II membrane particles as a tool for studying photosynthetic oxygen evolution. Photosynth. Res. 65 (2000) 41-52
    • (2000) Photosynth. Res. , vol.65 , pp. 41-52
    • Pospíšil, P.1    Dau, H.2
  • 29
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 181-364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 30
    • 0026795470 scopus 로고
    • Difference FT-IR study of a novel biochemical preparation of photosystem II
    • MacDonald G.M., and Barry B.A. Difference FT-IR study of a novel biochemical preparation of photosystem II. Biochemistry 31 (1992) 9848-9856
    • (1992) Biochemistry , vol.31 , pp. 9848-9856
    • MacDonald, G.M.1    Barry, B.A.2
  • 31
    • 0028120538 scopus 로고
    • Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by fourier transform infrared spectroscopy
    • Fabian H., Schultz C., Backmann J., Hahn U., Saenger W., Mantsch H.H., and Naumann D. Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by fourier transform infrared spectroscopy. Biochemistry 33 (1994) 10725-10730
    • (1994) Biochemistry , vol.33 , pp. 10725-10730
    • Fabian, H.1    Schultz, C.2    Backmann, J.3    Hahn, U.4    Saenger, W.5    Mantsch, H.H.6    Naumann, D.7
  • 32
    • 0026627740 scopus 로고
    • Detection of structural changes upon Sl-to-S2 transition in the oxygen-evolving manganese cluster in photosystem II by light-induced fourier transform infrared difference spectroscopy
    • Noguchi T., Ono T.A., and Inoue Y. Detection of structural changes upon Sl-to-S2 transition in the oxygen-evolving manganese cluster in photosystem II by light-induced fourier transform infrared difference spectroscopy. Biochemistry 31 (1992) 5953-5956
    • (1992) Biochemistry , vol.31 , pp. 5953-5956
    • Noguchi, T.1    Ono, T.A.2    Inoue, Y.3
  • 33
    • 0002336495 scopus 로고
    • Biomembrane structure from FT-IR spectroscopy
    • Jackson M., and Mantsch H.H. Biomembrane structure from FT-IR spectroscopy. Spectrochim. Acta Rev. 15 (1993) 53-69
    • (1993) Spectrochim. Acta Rev. , vol.15 , pp. 53-69
    • Jackson, M.1    Mantsch, H.H.2
  • 34
    • 0027765632 scopus 로고
    • Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles
    • Casals C., Miguel E., and Perez-Gil J. Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles. Biochem. J. 296 (1993) 585-593
    • (1993) Biochem. J. , vol.296 , pp. 585-593
    • Casals, C.1    Miguel, E.2    Perez-Gil, J.3
  • 35
    • 0242353812 scopus 로고    scopus 로고
    • Predissociated dimers and molten globule monomers in the equilibrium unfolding of yeast glutathione reductase
    • Louzada P.R., Sebollela A., Scaramello M.E., and Ferreira S.T. Predissociated dimers and molten globule monomers in the equilibrium unfolding of yeast glutathione reductase. Biophys. J. 85 (2003) 3255-3261
    • (2003) Biophys. J. , vol.85 , pp. 3255-3261
    • Louzada, P.R.1    Sebollela, A.2    Scaramello, M.E.3    Ferreira, S.T.4
  • 38
    • 0035140333 scopus 로고    scopus 로고
    • N bromosuccinimide modification of tryptophan 241 at the C-terminus of the manganese stabilizing protein of plant photosystem II influences its structure and function
    • Yong Y., Rong L., Chunhe X., Kangcheng R., Yunkang S., and Govindjee. N bromosuccinimide modification of tryptophan 241 at the C-terminus of the manganese stabilizing protein of plant photosystem II influences its structure and function. Physiol. Plant 111 (2001) 108-115
    • (2001) Physiol. Plant , vol.111 , pp. 108-115
    • Yong, Y.1    Rong, L.2    Chunhe, X.3    Kangcheng, R.4    Yunkang, S.5    Govindjee6


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