메뉴 건너뛰기




Volumn 9, Issue , 2011, Pages

Cellular oxido-reductive proteins of Chlamydomonas reinhardtii control the biosynthesis of silver nanoparticles

Author keywords

[No Author keywords available]

Indexed keywords

ATP SYNTHASE; CELL-FREE EXTRACTS; CELLULAR PROTEINS; CHLAMYDOMONAS REINHARDTII; IN-VITRO; IN-VIVO; MALDI-MS-MS; MODEL SYSTEM; MOLECULAR MACHINERY; MOLECULAR MECHANISM; MONODISPERSITY; SDS-PAGE ANALYSIS; SHAPE AND SIZE; SILVER NANOPARTICLES; SIZE RANGES; SUPER OXIDE DISMUTASE; SYNTHESIS RATE; UNICELLULAR ALGA; UNIFORM DISTRIBUTION;

EID: 82755167830     PISSN: None     EISSN: 14773155     Source Type: Journal    
DOI: 10.1186/1477-3155-9-56     Document Type: Article
Times cited : (128)

References (51)
  • 1
    • 77953218309 scopus 로고    scopus 로고
    • Potential use of silver nanoparticles on pathogenic bacteria, their toxicity and possible mechanisms of action
    • Durán N, Marcato PD, Conti RD, Alves OL, Costa FTM, Brocchi M. Potential use of silver nanoparticles on pathogenic bacteria, their toxicity and possible mechanisms of action. J Braz Chem Soc 2010, 21:949-959.
    • (2010) J Braz Chem Soc , vol.21 , pp. 949-959
    • Durán, N.1    Marcato, P.D.2    Conti, R.D.3    Alves, O.L.4    Costa, F.T.M.5    Brocchi, M.6
  • 2
    • 45849132429 scopus 로고    scopus 로고
    • New aspects of nanopharmaceutical delivery systems
    • Marcato PD, Duran N. New aspects of nanopharmaceutical delivery systems. J Nanosci Nanotechnol 2008, 8:2216-2229.
    • (2008) J Nanosci Nanotechnol , vol.8 , pp. 2216-2229
    • Marcato, P.D.1    Duran, N.2
  • 3
    • 57249095780 scopus 로고    scopus 로고
    • Silver nanoparticles as a new generation of antimicrobials
    • Rai M, Yadav A, Gade A. Silver nanoparticles as a new generation of antimicrobials. Biotechnol Adv 2009, 27:76-83.
    • (2009) Biotechnol Adv , vol.27 , pp. 76-83
    • Rai, M.1    Yadav, A.2    Gade, A.3
  • 4
    • 85123316636 scopus 로고    scopus 로고
    • Nanomaterials and nanoparticles: sources and toxicity
    • Buzea C, Pacheco II, Robbie K. Nanomaterials and nanoparticles: sources and toxicity. Biointerphases 2007, 2:MR17-71.
    • (2007) Biointerphases , vol.2
    • Buzea, C.1    Pacheco, I.I.2    Robbie, K.3
  • 5
    • 0020346753 scopus 로고
    • Magnetotactic bacteria
    • Blakemore RP. Magnetotactic bacteria. Annu Rev Microbiol 1982, 36:217-238.
    • (1982) Annu Rev Microbiol , vol.36 , pp. 217-238
    • Blakemore, R.P.1
  • 6
    • 0037814710 scopus 로고    scopus 로고
    • Polycationic peptides from diatom biosilica that direct silica nanosphere formation
    • Kroger N, Deutzmann R, Sumper M. Polycationic peptides from diatom biosilica that direct silica nanosphere formation. Science 1999, 286:1129-1132.
    • (1999) Science , vol.286 , pp. 1129-1132
    • Kroger, N.1    Deutzmann, R.2    Sumper, M.3
  • 9
    • 79958120530 scopus 로고    scopus 로고
    • Mechanistic aspects in the biogenic synthesis of extracellular metal nanoparticles by peptides, bacteria, fungi, and plants
    • Duran N, Marcato PD, Duran M, Yadav A, Gade A, Rai M. Mechanistic aspects in the biogenic synthesis of extracellular metal nanoparticles by peptides, bacteria, fungi, and plants. Appl Microbiol Biotechnol 2011, 90:1609-1624.
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 1609-1624
    • Duran, N.1    Marcato, P.D.2    Duran, M.3    Yadav, A.4    Gade, A.5    Rai, M.6
  • 10
    • 77952240650 scopus 로고    scopus 로고
    • Mycogenic metal nanoparticles: progress and applications
    • Gade A, Ingle A, Whiteley C, Rai M. Mycogenic metal nanoparticles: progress and applications. Biotechnol Lett 2010, 32:593-600.
    • (2010) Biotechnol Lett , vol.32 , pp. 593-600
    • Gade, A.1    Ingle, A.2    Whiteley, C.3    Rai, M.4
  • 12
    • 68149160866 scopus 로고    scopus 로고
    • The mechanism of metal nanoparticle formation in plants:limits on accumulation
    • Haverkamp RG, Marshall AT. The mechanism of metal nanoparticle formation in plants:limits on accumulation. J Nanopart Res 2009, 11:1453-1463.
    • (2009) J Nanopart Res , vol.11 , pp. 1453-1463
    • Haverkamp, R.G.1    Marshall, A.T.2
  • 13
    • 40149088170 scopus 로고    scopus 로고
    • On the formation and extent of uptake of silver nanoparticles by live plants
    • Harris AT, Bali R. On the formation and extent of uptake of silver nanoparticles by live plants. J Nanopart Res 2008, 10:691-695.
    • (2008) J Nanopart Res , vol.10 , pp. 691-695
    • Harris, A.T.1    Bali, R.2
  • 15
    • 26844467301 scopus 로고    scopus 로고
    • Mechanistic aspects of biosynthesis of silver nanoparticles by several Fusarium oxysporum strains
    • Duran N, Marcato PD, Alves OL, Souza GI, Esposito E. Mechanistic aspects of biosynthesis of silver nanoparticles by several Fusarium oxysporum strains. J Nanobiotechnology 2005, 3:8.
    • (2005) J Nanobiotechnology , vol.3 , pp. 8
    • Duran, N.1    Marcato, P.D.2    Alves, O.L.3    Souza, G.I.4    Esposito, E.5
  • 17
    • 47749086298 scopus 로고    scopus 로고
    • Mycosynthesis of silver nanoparticles using the fungus Fusarium acuminatum and its activity against some human pathogenic bacteria
    • Ingle A, Gade A, Pierrat S, Sonnichsen C, Rai M. Mycosynthesis of silver nanoparticles using the fungus Fusarium acuminatum and its activity against some human pathogenic bacteria. Current Nanoscience 2008, 4:141-144.
    • (2008) Current Nanoscience , vol.4 , pp. 141-144
    • Ingle, A.1    Gade, A.2    Pierrat, S.3    Sonnichsen, C.4    Rai, M.5
  • 19
    • 0031903012 scopus 로고    scopus 로고
    • Novel anthraquinones from stationary cultures of Fusarium oxysporum
    • Baker R, Tatum J. Novel anthraquinones from stationary cultures of Fusarium oxysporum. J Ferment Bioeng 1998, 85:359-361.
    • (1998) J Ferment Bioeng , vol.85 , pp. 359-361
    • Baker, R.1    Tatum, J.2
  • 21
    • 34547468962 scopus 로고    scopus 로고
    • Green synthesis of silver nanoparticles using Capsicum annuum L. extract
    • Li S, Shen Y, Xie A, Yu X, Qiu L, Zhang L, Zhang Q. Green synthesis of silver nanoparticles using Capsicum annuum L. extract. Green Chem 2007, 9:852-858.
    • (2007) Green Chem , vol.9 , pp. 852-858
    • Li, S.1    Shen, Y.2    Xie, A.3    Yu, X.4    Qiu, L.5    Zhang, L.6    Zhang, Q.7
  • 23
    • 0242666859 scopus 로고    scopus 로고
    • Completely "green" synthesis and stabilization of metal nanoparticles
    • Raveendran P, Fu J, Wallen SL. Completely "green" synthesis and stabilization of metal nanoparticles. J Am Chem Soc 2003, 125:13940-13941.
    • (2003) J Am Chem Soc , vol.125 , pp. 13940-13941
    • Raveendran, P.1    Fu, J.2    Wallen, S.L.3
  • 24
    • 0346783287 scopus 로고    scopus 로고
    • Geranium leaf assisted biosynthesis of silver nanoparticles
    • Shankar SS, Ahmad A, Sastry M. Geranium leaf assisted biosynthesis of silver nanoparticles. Biotechnol Prog 2003, 19:1627-1631.
    • (2003) Biotechnol Prog , vol.19 , pp. 1627-1631
    • Shankar, S.S.1    Ahmad, A.2    Sastry, M.3
  • 25
    • 2942564380 scopus 로고    scopus 로고
    • Rapid synthesis of Au, Ag, and bimetallic Au core-Ag shell nanoparticles using Neem (Azadirachta indica) leaf broth
    • Shankar SS, Rai A, Ahmad A, Sastry M. Rapid synthesis of Au, Ag, and bimetallic Au core-Ag shell nanoparticles using Neem (Azadirachta indica) leaf broth. J Colloid Interface Sci 2004, 275:496-502.
    • (2004) J Colloid Interface Sci , vol.275 , pp. 496-502
    • Shankar, S.S.1    Rai, A.2    Ahmad, A.3    Sastry, M.4
  • 26
    • 58149086014 scopus 로고    scopus 로고
    • Rapid biological synthesis of silver nanoparticles using plant leaf extracts
    • Song JY, Kim BS. Rapid biological synthesis of silver nanoparticles using plant leaf extracts. Bioprocess Biosyst Eng 2009, 32:79-84.
    • (2009) Bioprocess Biosyst Eng , vol.32 , pp. 79-84
    • Song, J.Y.1    Kim, B.S.2
  • 27
    • 67549119087 scopus 로고    scopus 로고
    • Controlled in-situ synthesis of silver nanoparticles in natural cellulose fibers toward highly efficient antimicrobial materials
    • Zhu C, Xue J, He J. Controlled in-situ synthesis of silver nanoparticles in natural cellulose fibers toward highly efficient antimicrobial materials. J Nanosci Nanotechnol 2009, 9:3067-3074.
    • (2009) J Nanosci Nanotechnol , vol.9 , pp. 3067-3074
    • Zhu, C.1    Xue, J.2    He, J.3
  • 28
    • 29444441417 scopus 로고    scopus 로고
    • Intracellular recovery of gold by microbial reduction of AuCl4- ions using the anaerobic bacterium Shewanella algae
    • Konishi Y, Tsukiyama T, Ohno K, Saitoh N, Nomura T, Nagamine S. Intracellular recovery of gold by microbial reduction of AuCl4- ions using the anaerobic bacterium Shewanella algae. Hydrometallurgy 2006, 81:24-29.
    • (2006) Hydrometallurgy , vol.81 , pp. 24-29
    • Konishi, Y.1    Tsukiyama, T.2    Ohno, K.3    Saitoh, N.4    Nomura, T.5    Nagamine, S.6
  • 29
    • 34447293548 scopus 로고    scopus 로고
    • Direct determination of oxidation state of gold deposits in metal-reducing bacterium Shewanella algae using X-ray absorption near-edge structure spectroscopy (XANES)
    • Konishi Y, Tsukiyama T, Saitoh N, Nomura T, Nagamine S, Takahashi Y, Uruga T. Direct determination of oxidation state of gold deposits in metal-reducing bacterium Shewanella algae using X-ray absorption near-edge structure spectroscopy (XANES). J Biosci Bioeng 2007, 103:568-571.
    • (2007) J Biosci Bioeng , vol.103 , pp. 568-571
    • Konishi, Y.1    Tsukiyama, T.2    Saitoh, N.3    Nomura, T.4    Nagamine, S.5    Takahashi, Y.6    Uruga, T.7
  • 30
    • 0037091278 scopus 로고    scopus 로고
    • Shape effect in plasmon resonance of indivisual colloidal silver nanoparticles
    • Mock JJ, Barbic M, Smith DR, DA S, S S. Shape effect in plasmon resonance of indivisual colloidal silver nanoparticles. J Chem Phys 2002, 116:6755-6759.
    • (2002) J Chem Phys , vol.116 , pp. 6755-6759
    • Mock, J.J.1    Barbic, M.2    Smith, D.R.3    Da, S.4    Shape, S.5
  • 32
    • 0013879307 scopus 로고
    • Histone specificity revealed by ammoniacal silver staining
    • Black MM, Ansley HR. Histone specificity revealed by ammoniacal silver staining. J Histochem Cytochem 1966, 14:177-181.
    • (1966) J Histochem Cytochem , vol.14 , pp. 177-181
    • Black, M.M.1    Ansley, H.R.2
  • 33
    • 0021765993 scopus 로고
    • Mechanism of silver staining of histones: evidence for involvement of clustered lysine residues
    • Kurosaki T, Tsutsui K, Tsutsui K, Aoyama K, Oda T. Mechanism of silver staining of histones: evidence for involvement of clustered lysine residues. Biochem Biophys Res Commun 1984, 123:729-734.
    • (1984) Biochem Biophys Res Commun , vol.123 , pp. 729-734
    • Kurosaki, T.1    Tsutsui, K.2    Tsutsui, K.3    Aoyama, K.4    Oda, T.5
  • 35
    • 21344432091 scopus 로고    scopus 로고
    • Histone peptide AKRHRK enhances H(2)O(2)-induced DNA damage and alters its site specificity
    • Midorikawa K, Murata M, Kawanishi S. Histone peptide AKRHRK enhances H(2)O(2)-induced DNA damage and alters its site specificity. Biochem Biophys Res Commun 2005, 333:1073-1077.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 1073-1077
    • Midorikawa, K.1    Murata, M.2    Kawanishi, S.3
  • 36
    • 22544459674 scopus 로고    scopus 로고
    • Ferredoxin-NADP+ reductase. Kinetics of electron transfer, transient intermediates, and catalytic activities studied by flash-absorption spectroscopy with isolated photosystem I and ferredoxin
    • Cassan N, Lagoutte B, Setif P. Ferredoxin-NADP+ reductase. Kinetics of electron transfer, transient intermediates, and catalytic activities studied by flash-absorption spectroscopy with isolated photosystem I and ferredoxin. J Biol Chem 2005, 280:25960-25972.
    • (2005) J Biol Chem , vol.280 , pp. 25960-25972
    • Cassan, N.1    Lagoutte, B.2    Setif, P.3
  • 39
    • 79951598005 scopus 로고    scopus 로고
    • Superoxide-Mediated Formation and Charging of Silver Nanoparticles
    • Jones AM, Garg S, He D, Pham AN, Waite TD. Superoxide-Mediated Formation and Charging of Silver Nanoparticles. Environ Sci Technol 2011, 45:1428-1434.
    • (2011) Environ Sci Technol , vol.45 , pp. 1428-1434
    • Jones, A.M.1    Garg, S.2    He, D.3    Pham, A.N.4    Waite, T.D.5
  • 40
    • 0032055764 scopus 로고    scopus 로고
    • The Calvin cycle enzyme sedoheptulose-1,7-bisphosphatase is encoded by a light-regulated gene in Chlamydomonas reinhardtii
    • Hahn D, Kaltenbach C, Kuck U. The Calvin cycle enzyme sedoheptulose-1,7-bisphosphatase is encoded by a light-regulated gene in Chlamydomonas reinhardtii. Plant Mol Biol 1998, 36:929-934.
    • (1998) Plant Mol Biol , vol.36 , pp. 929-934
    • Hahn, D.1    Kaltenbach, C.2    Kuck, U.3
  • 41
    • 0000765807 scopus 로고
    • Role of Light in the Regulation of Chloroplast Enzymes
    • Buchanan BB. Role of Light in the Regulation of Chloroplast Enzymes. Annual Review of Plant Physiology 1980, 31:341-374.
    • (1980) Annual Review of Plant Physiology , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 43
    • 77952334099 scopus 로고    scopus 로고
    • Proteomic analysis of the response of an acidophilic strain of Chlamydomonas sp. (Chlorophyta) to natural metal-rich water
    • Cid C, Garcia-Descalzo L, Casado-Lafuente V, Amils R, Aguilera A. Proteomic analysis of the response of an acidophilic strain of Chlamydomonas sp. (Chlorophyta) to natural metal-rich water. Proteomics 2010, 10:2026-2036.
    • (2010) Proteomics , vol.10 , pp. 2026-2036
    • Cid, C.1    Garcia-Descalzo, L.2    Casado-Lafuente, V.3    Amils, R.4    Aguilera, A.5
  • 44
    • 0023286729 scopus 로고
    • Expression of the nuclear encoded OEE1 protein is required for oxygen evolution and stability of photosystem II particles in Chlamydomonas reinhardtii
    • Mayfield SP, Bennoun P, Rochaix JD. Expression of the nuclear encoded OEE1 protein is required for oxygen evolution and stability of photosystem II particles in Chlamydomonas reinhardtii. Embo J 1987, 6:313-318.
    • (1987) Embo J , vol.6 , pp. 313-318
    • Mayfield, S.P.1    Bennoun, P.2    Rochaix, J.D.3
  • 45
    • 1442315673 scopus 로고    scopus 로고
    • The oxygen evolving enhancer protein 1 (OEE) of photosystem II in green algae exhibits thioredoxin activity
    • Heide H, Kalisz HM, Follmann H. The oxygen evolving enhancer protein 1 (OEE) of photosystem II in green algae exhibits thioredoxin activity. J Plant Physiol 2004, 161:139-149.
    • (2004) J Plant Physiol , vol.161 , pp. 139-149
    • Heide, H.1    Kalisz, H.M.2    Follmann, H.3
  • 46
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • Cedervall T, Lynch I, Lindman S, Berggard T, Thulin E, Nilsson H, Dawson KA, Linse S. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA 2007, 104:2050-2055.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggard, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 47
    • 70249141572 scopus 로고    scopus 로고
    • A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles
    • Rocker C, Potzl M, Zhang F, Parak WJ, Nienhaus GU. A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles. Nat Nanotechnol 2009, 4:577-580.
    • (2009) Nat Nanotechnol , vol.4 , pp. 577-580
    • Rocker, C.1    Potzl, M.2    Zhang, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 48
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp F, Karas M, Beavis RC, Chait BT. Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal Chem 1991, 63:1193A-1203A.
    • (1991) Anal Chem , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 49
    • 0343775584 scopus 로고    scopus 로고
    • Ionization in matrix-assisted laser desorption/ionization: singly charged molecular ions are the lucky survivors
    • Karas M, Gluckmann M, Schafer J. Ionization in matrix-assisted laser desorption/ionization: singly charged molecular ions are the lucky survivors. J Mass Spectrom 2000, 35:1-12.
    • (2000) J Mass Spectrom , vol.35 , pp. 1-12
    • Karas, M.1    Gluckmann, M.2    Schafer, J.3
  • 50
    • 0031871699 scopus 로고    scopus 로고
    • Suppression effects in enzymatic peptide ladder sequencing using ultraviolet - matrix assisted laser desorption/ionization - mass spectormetry
    • Kratzer R, Eckerskorn C, Karas M, Lottspeich F. Suppression effects in enzymatic peptide ladder sequencing using ultraviolet - matrix assisted laser desorption/ionization - mass spectormetry. Electrophoresis 1998, 19:1910-1919.
    • (1998) Electrophoresis , vol.19 , pp. 1910-1919
    • Kratzer, R.1    Eckerskorn, C.2    Karas, M.3    Lottspeich, F.4
  • 51
    • 0033214277 scopus 로고    scopus 로고
    • The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins
    • Krause E, Wenschuh H, Jungblut PR. The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins. Anal Chem 1999, 71:4160-4165.
    • (1999) Anal Chem , vol.71 , pp. 4160-4165
    • Krause, E.1    Wenschuh, H.2    Jungblut, P.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.