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Volumn 7, Issue 4, 2012, Pages

Optimized expression and purification for high-activity preparations of algal [FeFe]-hydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

FD HYDA1 FUSION PROTEIN; HYBRID PROTEIN; HYDA1 HYDROGENASE; HYDROGEN; OXIDOREDUCTASE; UNCLASSIFIED DRUG; BLOOD CLOTTING FACTOR 10A; FERREDOXIN; HYDROGENASE; IRON HYDROGENASE; IRON SULFUR PROTEIN; PROTEINASE; TEV PROTEASE;

EID: 84860362239     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035886     Document Type: Article
Times cited : (33)

References (34)
  • 2
    • 77953340990 scopus 로고    scopus 로고
    • Photobiological production of hydrogen gas as a biofuel
    • McKinlay JB, Harwood CS, (2010) Photobiological production of hydrogen gas as a biofuel. Curr Opin Biotechnol 21: 244-251.
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 244-251
    • McKinlay, J.B.1    Harwood, C.S.2
  • 5
    • 46549086572 scopus 로고    scopus 로고
    • Photosynthetic Water-Splitting for Hydrogen Production
    • In: Wall JD, Harwood CS, Demain A, editors, Bioenergy: ASM Press
    • Seibert M, King PW, Posewitz MC, Melis A, Ghirardi ML, (2008) Photosynthetic Water-Splitting for Hydrogen Production. In: Wall JD, Harwood CS, Demain A, editors. Bioenergy: ASM Press.
    • (2008)
    • Seibert, M.1    King, P.W.2    Posewitz, M.C.3    Melis, A.4    Ghirardi, M.L.5
  • 8
    • 77953200590 scopus 로고    scopus 로고
    • The surprising diversity of clostridial hydrogenases: a comparative genomic perspective
    • Calusinska M, Happe T, Joris B, Wilmotte A, (2010) The surprising diversity of clostridial hydrogenases: a comparative genomic perspective. Microbiol 156: 1575-1588.
    • (2010) Microbiol , vol.156 , pp. 1575-1588
    • Calusinska, M.1    Happe, T.2    Joris, B.3    Wilmotte, A.4
  • 9
    • 77951976891 scopus 로고    scopus 로고
    • Biological hydrogen production: prospects and challenges
    • Lee H-S, Vermaas WFJ, Rittmann BE, (2010) Biological hydrogen production: prospects and challenges. Trends Biotechnol 28: 262-271.
    • (2010) Trends Biotechnol , vol.28 , pp. 262-271
    • Lee, H.-S.1    Vermaas, W.F.J.2    Rittmann, B.E.3
  • 11
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: an overview
    • Vignais PM, Billoud B, (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 107: 4206-4272.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 12
  • 13
    • 0142244261 scopus 로고    scopus 로고
    • Chemistry and the hydrogenases
    • Evans DJ, Pickett CJ, (2003) Chemistry and the hydrogenases. Chem Soc Rev 32: 268-275.
    • (2003) Chem Soc Rev , vol.32 , pp. 268-275
    • Evans, D.J.1    Pickett, C.J.2
  • 14
    • 34250902424 scopus 로고    scopus 로고
    • Hydrogenases and hydrogen photoproduction in oxygenic photosynthetic organisms
    • Ghirardi ML, Posewitz MC, Maness PC, Dubini A, Yu J, et al. (2007) Hydrogenases and hydrogen photoproduction in oxygenic photosynthetic organisms. Ann Rev Plant Biol 58: 71-91.
    • (2007) Ann Rev Plant Biol , vol.58 , pp. 71-91
    • Ghirardi, M.L.1    Posewitz, M.C.2    Maness, P.C.3    Dubini, A.4    Yu, J.5
  • 15
    • 84856261361 scopus 로고    scopus 로고
    • Catalytic turnover of [FeFe]-Hydrogenase based on single-molecule imaging
    • Madden C, Vaughn MD, Diez-Perez I, Brown KA, King PW, et al. (2011) Catalytic turnover of [FeFe]-Hydrogenase based on single-molecule imaging. J Am Chem Soc 134: 1577-1582.
    • (2011) J Am Chem Soc , vol.134 , pp. 1577-1582
    • Madden, C.1    Vaughn, M.D.2    Diez-Perez, I.3    Brown, K.A.4    King, P.W.5
  • 16
    • 81755171433 scopus 로고    scopus 로고
    • O2-reactions at the six-iron active site (H-cluster) in [FeFe]-hydrogenase
    • Lambertz C, Leidel N, Havelius KG, Noth J, Chernev P, et al. (2011) O2-reactions at the six-iron active site (H-cluster) in [FeFe]-hydrogenase. J Biol Chem 286: 40614-40623.
    • (2011) J Biol Chem , vol.286 , pp. 40614-40623
    • Lambertz, C.1    Leidel, N.2    Havelius, K.G.3    Noth, J.4    Chernev, P.5
  • 17
    • 57649243241 scopus 로고    scopus 로고
    • Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology
    • Armstrong FA, Belsey NA, Cracknell JA, Goldet G, Parkin A, et al. (2009) Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology. Chem Soc Rev 38: 36-51.
    • (2009) Chem Soc Rev , vol.38 , pp. 36-51
    • Armstrong, F.A.1    Belsey, N.A.2    Cracknell, J.A.3    Goldet, G.4    Parkin, A.5
  • 18
    • 78349259311 scopus 로고    scopus 로고
    • Controlled assembly of hydrogenase-CdTe nanocrystal hybrids for solar hydrogen production
    • Brown KA, Dayal S, Ai X, Rumbles G, King PW, (2010) Controlled assembly of hydrogenase-CdTe nanocrystal hybrids for solar hydrogen production. J Am Chem Soc 132: 9672-9680.
    • (2010) J Am Chem Soc , vol.132 , pp. 9672-9680
    • Brown, K.A.1    Dayal, S.2    Ai, X.3    Rumbles, G.4    King, P.W.5
  • 19
    • 73249146231 scopus 로고    scopus 로고
    • Visible light-driven H2 production by hydrogenases attached to dye-sensitized TiO2 nanoparticles
    • Reisner E, Powell DJ, Cavazza C, Fontecilla-Camps JC, Armstrong FA, (2009) Visible light-driven H2 production by hydrogenases attached to dye-sensitized TiO2 nanoparticles. J Am Chem Soc 131: 18457-18466.
    • (2009) J Am Chem Soc , vol.131 , pp. 18457-18466
    • Reisner, E.1    Powell, D.J.2    Cavazza, C.3    Fontecilla-Camps, J.C.4    Armstrong, F.A.5
  • 20
    • 72749100414 scopus 로고    scopus 로고
    • Recombinant and in vitro expression systems for hydrogenases: new frontiers in basic and applied studies for biological and synthetic H2 production
    • English CM, Eckert C, Brown K, Seibert M, King PW, (2009) Recombinant and in vitro expression systems for hydrogenases: new frontiers in basic and applied studies for biological and synthetic H2 production. Dalton Trans 45: 9970-9978.
    • (2009) Dalton Trans , vol.45 , pp. 9970-9978
    • English, C.M.1    Eckert, C.2    Brown, K.3    Seibert, M.4    King, P.W.5
  • 21
    • 18444393412 scopus 로고    scopus 로고
    • Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities
    • Girbal L, von Abendroth G, Winkler M, Benton PM, Meynial-Salles I, et al. (2005) Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities. Appl Environ Microbiol 71: 2777-2781.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 2777-2781
    • Girbal, L.1    von Abendroth, G.2    Winkler, M.3    Benton, P.M.4    Meynial-Salles, I.5
  • 22
    • 52749087981 scopus 로고    scopus 로고
    • Shewanella oneidensis: a new and efficient system for expression and maturation of heterologous [Fe-Fe] hydrogenase from Chlamydomonas reinhardtii
    • Sybirna K, Antoine T, Lindberg P, Fourmond V, Rousset M, et al. (2008) Shewanella oneidensis: a new and efficient system for expression and maturation of heterologous [Fe-Fe] hydrogenase from Chlamydomonas reinhardtii. BMC Biotechnol 8: 73.
    • (2008) BMC Biotechnol , vol.8 , pp. 73
    • Sybirna, K.1    Antoine, T.2    Lindberg, P.3    Fourmond, V.4    Rousset, M.5
  • 23
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • Posewitz MC, King PW, Smolinski SL, Zhang L, Seibert M, et al. (2004) Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J Biol Chem 279: 25711-25720.
    • (2004) J Biol Chem , vol.279 , pp. 25711-25720
    • Posewitz, M.C.1    King, P.W.2    Smolinski, S.L.3    Zhang, L.4    Seibert, M.5
  • 24
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • King PW, Posewitz MC, Ghirardi ML, Seibert M, (2006) Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system. J Bacteriol 188: 2163-2172.
    • (2006) J Bacteriol , vol.188 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 26
    • 79959329033 scopus 로고    scopus 로고
    • Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro
    • Yacoby I, Pochekailov S, Toporik H, Ghirardi ML, King PW, et al. (2011) Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro. Proc Natl Acad Sci U S A 108: 9396-9401.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9396-9401
    • Yacoby, I.1    Pochekailov, S.2    Toporik, H.3    Ghirardi, M.L.4    King, P.W.5
  • 27
    • 0033939135 scopus 로고    scopus 로고
    • Controlled intracellular processing of fusion proteins by TEV protease
    • Kapust RB, Waugh DS, (2000) Controlled intracellular processing of fusion proteins by TEV protease. Protein Expr Purif 19: 312-318.
    • (2000) Protein Expr Purif , vol.19 , pp. 312-318
    • Kapust, R.B.1    Waugh, D.S.2
  • 28
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust RB, Tozser J, Fox JD, Anderson DE, Cherry S, et al. (2001) Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng 14: 993-1000.
    • (2001) Protein Eng , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5
  • 29
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster
    • Nakamura M, Saeki K, Takahashi Y, (1999) Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster. J Biochem 126: 10-18.
    • (1999) J Biochem , vol.126 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 30
    • 55049112510 scopus 로고    scopus 로고
    • Optimized over-expression of [FeFe] hydrogenases with high specific activity in Clostridium acetobutylicum
    • von Abendroth G, Stripp S, Silakov A, Croux C, Soucaille P, et al. (2008) Optimized over-expression of [FeFe] hydrogenases with high specific activity in Clostridium acetobutylicum. Int J Hydrogen Energy 33: 6076-6081.
    • (2008) Int J Hydrogen Energy , vol.33 , pp. 6076-6081
    • von Abendroth, G.1    Stripp, S.2    Silakov, A.3    Croux, C.4    Soucaille, P.5
  • 31
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish WW, (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol 158: 357-364.
    • (1988) Methods Enzymol , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 32
    • 69049116388 scopus 로고    scopus 로고
    • Spectroelectrochemical characterization of the active site of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii
    • Silakov A, Kamp C, Reijerse E, Happe T, Lubitz W, (2009) Spectroelectrochemical characterization of the active site of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii. Biochemistry 48: 7780-7786.
    • (2009) Biochemistry , vol.48 , pp. 7780-7786
    • Silakov, A.1    Kamp, C.2    Reijerse, E.3    Happe, T.4    Lubitz, W.5
  • 33
    • 43049112041 scopus 로고    scopus 로고
    • Isolation and first EPR characterization of the [FeFe]-hydrogenases from green algae
    • Kamp C, Silakov A, Winkler M, Reijerse EJ, Lubitz W, et al. (2008) Isolation and first EPR characterization of the [FeFe]-hydrogenases from green algae. Biochim Biophys Acta 1777: 410-416.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 410-416
    • Kamp, C.1    Silakov, A.2    Winkler, M.3    Reijerse, E.J.4    Lubitz, W.5
  • 34
    • 0027153213 scopus 로고
    • Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
    • Happe T, Naber JD, (1993) Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii. Eur J Biochem 214: 475-481.
    • (1993) Eur J Biochem , vol.214 , pp. 475-481
    • Happe, T.1    Naber, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.