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Volumn , Issue , 2012, Pages 25-53

Photosynthetic hydrogen production: Mechanisms and approaches

Author keywords

ATP; Ferredoxin; Gloeocapsa; Hydrogen production; Hydrogenases; NADPH; Nitrogenases; Nostoc; Oxygen evolving complex; Photosystem i; Photosystem ii; Spirulina; Synechococcus; Synechocystis

Indexed keywords


EID: 84860374523     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.2174/978160805224011201010025     Document Type: Chapter
Times cited : (15)

References (203)
  • 1
    • 0033618581 scopus 로고    scopus 로고
    • A realizable renewable energy future
    • Turner JA. A realizable renewable energy future. Science 1999; 285: 687-9.
    • (1999) Science , vol.285 , pp. 687-689
    • Turner, J.A.1
  • 2
    • 33748291968 scopus 로고    scopus 로고
    • Toward a more secure and cleaner energy future for America: national hydrogen energy roadmap; production, delivery, storage, conversion, applications, public education and outreach
    • .S. Department of Energy. Washington, DC
    • Abraham S. Toward a more secure and cleaner energy future for America: national hydrogen energy roadmap; production, delivery, storage, conversion, applications, public education and outreach. U.S. Department of Energy. Washington, DC, 2002.
    • (2002)
    • Abraham, S.1
  • 4
    • 59549086665 scopus 로고    scopus 로고
    • (Eds) Photosynthesis from molecular perspectives: towards future energy production
    • Allakhverdiev SI, Casal JJ, Nagata T. (Eds) Photosynthesis from molecular perspectives: towards future energy production. Photochem Photobiol Sci 2009; 8: 137-8.
    • (2009) Photochem Photobiol Sci , vol.8 , pp. 137-138
    • Allakhverdiev, S.I.1    Casal, J.J.2    Nagata, T.3
  • 6
    • 78649688952 scopus 로고    scopus 로고
    • Photosynthetic energy conversion: hydrogen photoproduction by natural and biomimetic systems
    • In: Mukherjee A, Ed. Biomimetics, Learning from nature. Vienna, Austria: IN-TECH
    • Allakhverdiev SI, Kreslavski VD, Thavasi V, et al. Photosynthetic energy conversion: hydrogen photoproduction by natural and biomimetic systems. In: Mukherjee A, Ed. Biomimetics, Learning from nature. Vienna, Austria: IN-TECH 2010; pp. 49-75.
    • (2010) , pp. 49-75
    • Allakhverdiev, S.I.1    Kreslavski, V.D.2    Thavasi, V.3
  • 8
    • 49649115311 scopus 로고    scopus 로고
    • Recent developments in biological hydrogen production processes
    • Das D, Khanna N, Veziroǧlu TN. Recent developments in biological hydrogen production processes. Chem Ind Chem Eng Q 2008; 14: 57-67.
    • (2008) Chem Ind Chem Eng Q , vol.14 , pp. 57-67
    • Das, D.1    Khanna, N.2    Veziroǧlu, T.N.3
  • 10
    • 59549104858 scopus 로고    scopus 로고
    • Hydrogen photoproduction by use of photosynthetic organisms and biomimetic systems
    • Allakhverdiev SI, Kreslavski VD, Thavasi V, et al. Hydrogen photoproduction by use of photosynthetic organisms and biomimetic systems. Photochem Photobiol Sci 2009; 8: 148-56.
    • (2009) Photochem Photobiol Sci , vol.8 , pp. 148-156
    • Allakhverdiev, S.I.1    Kreslavski, V.D.2    Thavasi, V.3
  • 11
    • 0004268113 scopus 로고    scopus 로고
    • Photosynthesis
    • 6th Edition. Cambridge, UK: Cambridge University Press
    • Hall DO, Rao KK. Photosynthesis. 6th Edition. Cambridge, UK: Cambridge University Press 1999.
    • (1999)
    • Hall, D.O.1    Rao, K.K.2
  • 12
    • 0004279464 scopus 로고    scopus 로고
    • Molecular mechanisms of photosynthesis
    • Oxford, UK: Blackwell Science
    • Blankenship RE. Molecular mechanisms of photosynthesis. Oxford, UK: Blackwell Science 2002.
    • (2002)
    • Blankenship, R.E.1
  • 13
    • 0000148282 scopus 로고
    • The potential applications of cyanobacterial photosynthesis for clean technologies
    • Hall DO, Markov SA, Watanabe Y, Rao K. The potential applications of cyanobacterial photosynthesis for clean technologies. Photosynth Res 1995; 46: 159-67.
    • (1995) Photosynth Res , vol.46 , pp. 159-167
    • Hall, D.O.1    Markov, S.A.2    Watanabe, Y.3    Rao, K.4
  • 14
    • 0033759410 scopus 로고    scopus 로고
    • Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii
    • Melis A, Zhang L, Forestier M, Ghirardi M, Seibert M. Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii. Plant Physiol 2000; 122: 127-36.
    • (2000) Plant Physiol , vol.122 , pp. 127-136
    • Melis, A.1    Zhang, L.2    Forestier, M.3    Ghirardi, M.4    Seibert, M.5
  • 15
    • 84889656305 scopus 로고    scopus 로고
    • Photobiological hydrogen production by cyanobacteria utilizing nitrogenase systems-present status and future development
    • In: Miyake J, Igarashi Y, Rögner M, Eds. Biohydrogen III. Renewable Energy System by Biological Energy Conversion. Amsterdam: Elsevier
    • Sakurai H, Masukawa H, Dawar S, Yoshino F. Photobiological hydrogen production by cyanobacteria utilizing nitrogenase systems-present status and future development. In: Miyake J, Igarashi Y, Rögner M, Eds. Biohydrogen III. Renewable Energy System by Biological Energy Conversion. Amsterdam: Elsevier 2004; pp. 84-93.
    • (2004) , pp. 84-93
    • Sakurai, H.1    Masukawa, H.2    Dawar, S.3    Yoshino, F.4
  • 17
    • 0006889984 scopus 로고
    • Purple phototrophic bacteria
    • In: Shively JM, Barton LL, Eds. Variations in autotrophic life. London: Academic Press
    • Drews G, Imhoff JF. Purple phototrophic bacteria. In: Shively JM, Barton LL, Eds. Variations in autotrophic life. London: Academic Press 1991; pp. 51-97.
    • (1991) , pp. 51-97
    • Drews, G.1    Imhoff, J.F.2
  • 18
    • 33846213610 scopus 로고    scopus 로고
    • The prospect of purple non-sulfur (PNS) photosynthetic bacteria for hydrogen production: the present state of art
    • Basak N, Das D. The prospect of purple non-sulfur (PNS) photosynthetic bacteria for hydrogen production: the present state of art. World J Microbiol Biotech 2007; 23: 31-42.
    • (2007) World J Microbiol Biotech , vol.23 , pp. 31-42
    • Basak, N.1    Das, D.2
  • 19
    • 0036827180 scopus 로고    scopus 로고
    • Aspects of the metabolism of hydrogen production by Rhodobacter sphaeroides
    • Koku H, Eroglu I, Gunduz U, Yucel M, Turker L. Aspects of the metabolism of hydrogen production by Rhodobacter sphaeroides. Int J Hydrogen Energy 2002; 27: 1315-29.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1315-1329
    • Koku, H.1    Eroglu, I.2    Gunduz, U.3    Yucel, M.4    Turker, L.5
  • 20
    • 33746928716 scopus 로고    scopus 로고
    • Integrated biological hydrogen production
    • Melis A., Melnicki MR. Integrated biological hydrogen production. Int J Hydrogen Energy 2006; 31: 1563-73.
    • (2006) Int J Hydrogen Energy , vol.31 , pp. 1563-1573
    • Melis, A.1    Melnicki, M.R.2
  • 22
    • 36849071982 scopus 로고    scopus 로고
    • Photosystem II: Structure and mechanism of the water: plastoquinone oxidoreductase
    • Kern J, Renger G. Photosystem II: Structure and mechanism of the water: plastoquinone oxidoreductase. Photosynth Res 2007; 94: 183-202.
    • (2007) Photosynth Res , vol.94 , pp. 183-202
    • Kern, J.1    Renger, G.2
  • 23
    • 42149109765 scopus 로고    scopus 로고
    • Crystal structure of the oxygen-evolving complex of photosystem II
    • Barber, J. Crystal structure of the oxygen-evolving complex of photosystem II. Inorg Chem 2008; 47: 1700-10.
    • (2008) Inorg Chem , vol.47 , pp. 1700-1710
    • Barber, J.1
  • 24
    • 0014202070 scopus 로고
    • Chemiosmotic hypothesis of oxidative phosphorylation
    • Mitchell P, Moyle J. Chemiosmotic hypothesis of oxidative phosphorylation. Nature 1967; 213: 137-9.
    • (1967) Nature , vol.213 , pp. 137-139
    • Mitchell, P.1    Moyle, J.2
  • 25
    • 0011239391 scopus 로고
    • The path of carbon in photosynthesis
    • Bassham J, Benson A, Calvin M. The path of carbon in photosynthesis. J Biol Chem 1950; 185: 781-7.
    • (1950) J Biol Chem , vol.185 , pp. 781-787
    • Bassham, J.1    Benson, A.2    Calvin, M.3
  • 26
    • 0000281326 scopus 로고
    • Bacterial photosynthesis
    • In: Antony C, Ed. Bacterial energy transduction. London: Academic Press
    • Jackson JB. Bacterial photosynthesis. In: Antony C, Ed. Bacterial energy transduction. London: Academic Press 1988; pp. 317-76.
    • (1988) , pp. 317-376
    • Jackson, J.B.1
  • 27
    • 0001695168 scopus 로고
    • Functional conjunction of hydrogenase with photosystem II in whole cells of Chlamydomonas reinhardtii mutants
    • Boichenko VA, Allakhverdiev SI, Ladygin VG, Klimov VV. Functional conjunction of hydrogenase with photosystem II in whole cells of Chlamydomonas reinhardtii mutants. Dokl AN SSSR 1986; 290: 995-8.
    • (1986) Dokl AN SSSR , vol.290 , pp. 995-998
    • Boichenko, V.A.1    Allakhverdiev, S.I.2    Ladygin, V.G.3    Klimov, V.V.4
  • 28
    • 0013616452 scopus 로고
    • Hydrogen evolution by subchloroplast preparations of photosystem II from pea and spinach
    • Maltsev SV, Allakhverdiev SI, Klimov VV, Krasnovsky AA. Hydrogen evolution by subchloroplast preparations of photosystem II from pea and spinach. FEBS Lett 1988; 240: 1-5.
    • (1988) FEBS Lett , vol.240 , pp. 1-5
    • Maltsev, S.V.1    Allakhverdiev, S.I.2    Klimov, V.V.3    Krasnovsky, A.A.4
  • 31
    • 34247610894 scopus 로고    scopus 로고
    • Promoting R & D in photobiological hydrogen production utilizing mariculture-raised cyanobacteria
    • Sakurai H, Masukawa H. Promoting R & D in photobiological hydrogen production utilizing mariculture-raised cyanobacteria. Mar Biotechnol 2007; 9: 128-45.
    • (2007) Mar Biotechnol , vol.9 , pp. 128-145
    • Sakurai, H.1    Masukawa, H.2
  • 32
    • 66149110298 scopus 로고    scopus 로고
    • Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation
    • Hoffman BM, Dean DR, Seefeldt LC. Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation. Acc Chem Res 2009; 42: 609-19.
    • (2009) Acc Chem Res , vol.42 , pp. 609-619
    • Hoffman, B.M.1    Dean, D.R.2    Seefeldt, L.C.3
  • 34
    • 0032216314 scopus 로고    scopus 로고
    • Hydrogen metabolism in organisms with oxygenic photosynthesis: hydrogenases as important regulatory devices for a proper redox poising?
    • Appel, J, Schulz R. Hydrogen metabolism in organisms with oxygenic photosynthesis: hydrogenases as important regulatory devices for a proper redox poising? J Photoch Photobio B 1998; 47: 1-11.
    • (1998) J Photoch Photobio B , vol.47 , pp. 1-11
    • Appel, J.1    Schulz, R.2
  • 35
    • 44449159969 scopus 로고    scopus 로고
    • Hydrogenases and H(+)-reduction in primary energy conservation
    • Vignais PM. Hydrogenases and H(+)-reduction in primary energy conservation. Results Probl Cell Differ 2008; 45: 223-52.
    • (2008) Results Probl Cell Differ , vol.45 , pp. 223-252
    • Vignais, P.M.1
  • 36
    • 0036836471 scopus 로고    scopus 로고
    • Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients
    • Cournac L, Mus F, Bernard L, Guedeney G, Vignais P, Peltier G. Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients. Int J Hydrogen Energy 2002; 27: 1229-37.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1229-1237
    • Cournac, L.1    Mus, F.2    Bernard, L.3    Guedeney, G.4    Vignais, P.5    Peltier, G.6
  • 37
    • 0002680858 scopus 로고
    • Regulation of nitrogen fixation genes
    • In: Blankenship RE, Madigan MT, Bauer CE, Eds. Anoxygenic photosynthetic bacteria. Netherlands: Kluwer Academic Press
    • Kranz RG, Cullen PJ. Regulation of nitrogen fixation genes. In: Blankenship RE, Madigan MT, Bauer CE, Eds. Anoxygenic photosynthetic bacteria. Netherlands: Kluwer Academic Press 1995; pp. 1191-208.
    • (1995) , pp. 1191-1208
    • Kranz, R.G.1    Cullen, P.J.2
  • 38
    • 0033777079 scopus 로고    scopus 로고
    • Nitrogenase: standing at the crossroads
    • Rees DC, Howard JB. Nitrogenase: standing at the crossroads. Curr Opin Chem Biol 2000; 4: 559-66.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 559-566
    • Rees, D.C.1    Howard, J.B.2
  • 39
    • 0142106006 scopus 로고    scopus 로고
    • Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase
    • Igarashi RY, Seefeldt LC. Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase. Crit Rev Biochem Mol Biol 2003; 38: 351-84.
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 351-384
    • Igarashi, R.Y.1    Seefeldt, L.C.2
  • 42
    • 70449612704 scopus 로고    scopus 로고
    • Biophotolysis-based hydrogen production by cyanobacteria and green microalgae
    • In: Mendes-Vilas A, Ed. Communicating current research and educational topics and trends in applied microbiology. Badajoz, Spain: Formatex
    • Yu J, Takahashi P. Biophotolysis-based hydrogen production by cyanobacteria and green microalgae. In: Mendes-Vilas A, Ed. Communicating current research and educational topics and trends in applied microbiology. Badajoz, Spain: Formatex 2007; pp. 79-89.
    • (2007) , pp. 79-89
    • Yu, J.1    Takahashi, P.2
  • 43
    • 0001090049 scopus 로고
    • Energetic efficiency of hydrogen photoevolution by algal water splitting
    • Greenbaum E. Energetic efficiency of hydrogen photoevolution by algal water splitting. Biophys J 1988; 54: 365-8.
    • (1988) Biophys J , vol.54 , pp. 365-368
    • Greenbaum, E.1
  • 44
    • 0021526164 scopus 로고
    • Stimulation of hydrogen photoproduction in algae by removal of oxygen by reagents that combine reversibly with oxygen
    • Rosenkranz A, Krasna AJ. Stimulation of hydrogen photoproduction in algae by removal of oxygen by reagents that combine reversibly with oxygen. Biotechnol Bioeng 1984; 26: 1334-42.
    • (1984) Biotechnol Bioeng , vol.26 , pp. 1334-1342
    • Rosenkranz, A.1    Krasna, A.J.2
  • 45
    • 34548528653 scopus 로고    scopus 로고
    • Photosynthetic H2 metabolism in Chlamydomonas reinhardtii (unicellular green algae)
    • Melis A. Photosynthetic H2 metabolism in Chlamydomonas reinhardtii (unicellular green algae). Planta 2007; 226: 1075-86.
    • (2007) Planta , vol.226 , pp. 1075-1086
    • Melis, A.1
  • 47
    • 0036827191 scopus 로고    scopus 로고
    • Biological hydrogen production; fundamentals and limiting processes
    • Hallenbeck PC, Benemann JR. Biological hydrogen production; fundamentals and limiting processes. Int J Hydrogen Energy 2002; 27: 1185-93.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1185-1193
    • Hallenbeck, P.C.1    Benemann, J.R.2
  • 48
    • 0026684361 scopus 로고
    • Oxygen relations of nitrogen fixation in cyanobacteria
    • Fay P. Oxygen relations of nitrogen fixation in cyanobacteria. Microbiol Rev 1992; 56: 340-73.
    • (1992) Microbiol Rev , vol.56 , pp. 340-373
    • Fay, P.1
  • 49
    • 0028352958 scopus 로고
    • Interaction between the environment, intermediary metabolism and cellular differentiation in a filamentous cyanobacterium
    • Campbell D. Interaction between the environment, intermediary metabolism and cellular differentiation in a filamentous cyanobacterium. B I Pasteur 1994; 92: 27-43.
    • (1994) B I Pasteur , vol.92 , pp. 27-43
    • Campbell, D.1
  • 50
    • 0005235480 scopus 로고    scopus 로고
    • Heterocyst differentiation and nitrogen fixation in cyanobacteria
    • In: Elmerich C, Kondorosi A, Newton WE, Eds. Biological Nitrogen Fixation for the 21st Century. Dordrecht: Kluwer
    • Haselkorn R, Schlictman D, Jones K, Buikema WJ. Heterocyst differentiation and nitrogen fixation in cyanobacteria. In: Elmerich C, Kondorosi A, Newton WE, Eds. Biological Nitrogen Fixation for the 21st Century. Dordrecht: Kluwer 1997; pp. 93-96.
    • (1997) , pp. 93-96
    • Haselkorn, R.1    Schlictman, D.2    Jones, K.3    Buikema, W.J.4
  • 51
    • 0030458712 scopus 로고    scopus 로고
    • Heterocyst formation
    • Wolk CP. Heterocyst formation. Annu Rev Genet 1996; 30: 59-78.
    • (1996) Annu Rev Genet , vol.30 , pp. 59-78
    • Wolk, C.P.1
  • 53
    • 0035062385 scopus 로고    scopus 로고
    • N2 fixation in phototrophs: adaptation to a specialized way of life
    • Gallon JR. N2 fixation in phototrophs: adaptation to a specialized way of life. Plant Soil. 2001; 230: 39-48.
    • (2001) Plant Soil. , vol.230 , pp. 39-48
    • Gallon, J.R.1
  • 54
    • 0022972183 scopus 로고
    • Strategy by which nitrogen-fixing unicellular cyanobacteria grow photoautotrophically
    • Mitsui A, Kumazawa S, Takahashi A, Ikemoto H, Cao S, Arai T. Strategy by which nitrogen-fixing unicellular cyanobacteria grow photoautotrophically. Nature 1986; 323: 720-2.
    • (1986) Nature , vol.323 , pp. 720-722
    • Mitsui, A.1    Kumazawa, S.2    Takahashi, A.3    Ikemoto, H.4    Cao, S.5    Arai, T.6
  • 55
    • 0019415777 scopus 로고
    • Aerobic nitrogen fixation in pure cultures of a benthic marine Oscillatoria (cyanobacteria)
    • Stal LJ, Krumbein WE. Aerobic nitrogen fixation in pure cultures of a benthic marine Oscillatoria (cyanobacteria). FEMS Microbiol Lett 1981; 11: 295-8.
    • (1981) FEMS Microbiol Lett , vol.11 , pp. 295-298
    • Stal, L.J.1    Krumbein, W.E.2
  • 56
    • 0001228605 scopus 로고
    • New type of N2-fixing unicellular cyanobacterium
    • Huang T-C, Chow T-J. New type of N2-fixing unicellular cyanobacterium. FEMS Microbiol Lett 1986; 50: 127-30.
    • (1986) FEMS Microbiol Lett , vol.50 , pp. 127-130
    • Huang, T.-C.1    Chow, T.-J.2
  • 58
    • 0019432223 scopus 로고
    • Acetylene reduction (nitrogen fixation) by cyanobacteria grown under alternating light-dark cycles
    • Mullineaux PM, Gallon JR, Chaplin AE. Acetylene reduction (nitrogen fixation) by cyanobacteria grown under alternating light-dark cycles. FEMS Microbiol Lett 1981; 10: 245-7.
    • (1981) FEMS Microbiol Lett , vol.10 , pp. 245-247
    • Mullineaux, P.M.1    Gallon, J.R.2    Chaplin, A.E.3
  • 59
    • 84941787599 scopus 로고
    • Fermentative and photochemical production of hydrogen in algae
    • Gaffron H, Rubin J. Fermentative and photochemical production of hydrogen in algae. J Gen Physiol 1942; 26: 219-40.
    • (1942) J Gen Physiol , vol.26 , pp. 219-240
    • Gaffron, H.1    Rubin, J.2
  • 60
    • 0001360267 scopus 로고
    • Isolation and characterization of a unicellular marine green alga exhibiting high activities in dark hydrogen production
    • Miura Y, Ohta S, Mano M, Miyamoto K. Isolation and characterization of a unicellular marine green alga exhibiting high activities in dark hydrogen production. Agric Biol Chem 1986; 50: 2837-44.
    • (1986) Agric Biol Chem , vol.50 , pp. 2837-2844
    • Miura, Y.1    Ohta, S.2    Mano, M.3    Miyamoto, K.4
  • 61
    • 0028556393 scopus 로고
    • Photosynthetic electron transport and anaerobic metabolism in purple non-sulfur photosynthetic bacteria
    • McEwan AG. Photosynthetic electron transport and anaerobic metabolism in purple non-sulfur photosynthetic bacteria. Antonie von Leeuwenhoek 1994; 66: 151-64.
    • (1994) Antonie von Leeuwenhoek , vol.66 , pp. 151-164
    • McEwan, A.G.1
  • 62
    • 38349058407 scopus 로고    scopus 로고
    • Modeling the electron transport chain of purple non- sulfur bacteria
    • Klamt S, Grammel H, Straube R, Ghosh R, Gilles ED. Modeling the electron transport chain of purple non- sulfur bacteria. Mol Syst Biol 2008; 4: 156-62.
    • (2008) Mol Syst Biol , vol.4 , pp. 156-162
    • Klamt, S.1    Grammel, H.2    Straube, R.3    Ghosh, R.4    Gilles, E.D.5
  • 63
    • 0036836419 scopus 로고    scopus 로고
    • Photohydrogen production using purple nonsulfur bacteria with hydrogen fermentation reactor effluent
    • Lee C, Chen P, Wang C, Tung Y. Photohydrogen production using purple nonsulfur bacteria with hydrogen fermentation reactor effluent. Int J Hydrogen Energy 2002; 27: 1309-13.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1309-1313
    • Lee, C.1    Chen, P.2    Wang, C.3    Tung, Y.4
  • 64
    • 33746886982 scopus 로고    scopus 로고
    • Non-thermal production of pure hydrogen from biomass
    • Claassen PA, de Vrije T. Non-thermal production of pure hydrogen from biomass. Int J Hydrogen Energy 2006; 31: 1416-23.
    • (2006) Int J Hydrogen Energy , vol.31 , pp. 1416-1423
    • Claassen, P.A.1    de Vrije, T.2
  • 65
    • 35748974830 scopus 로고    scopus 로고
    • Occurance, classification, and biological function of hydrogenases: an overview
    • Vignais PM, Billoud B. Occurance, classification, and biological function of hydrogenases: an overview. Chem Rev 2007; 107: 4206-72.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 67
    • 0031574022 scopus 로고    scopus 로고
    • Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
    • Higuchi Y, Yagi T, Yasuoka N. Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure 1997; 5: 1671-82.
    • (1997) Structure , vol.5 , pp. 1671-1682
    • Higuchi, Y.1    Yagi, T.2    Yasuoka, N.3
  • 68
    • 0031180380 scopus 로고    scopus 로고
    • Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
    • Montet Y, Amara P, Volbeda A, et al. Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics. Nat Struct Biol 1997; 4: 523-9.
    • (1997) Nat Struct Biol , vol.4 , pp. 523-529
    • Montet, Y.1    Amara, P.2    Volbeda, A.3
  • 70
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet Y, Piras C, Legrand P, Hatchikian CE, Fontecilla-Camps JC. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure 1999; 7: 13-23.
    • (1999) Structure , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-camps, J.C.5
  • 71
    • 0034846760 scopus 로고    scopus 로고
    • [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: primary sequence determination, crystallographic refinement at 1.8 Å and modelling studies of its interaction with the tetra-haem cytochrome c3
    • Matias PM, Soares CM, Saraiva LM, et al. [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: primary sequence determination, crystallographic refinement at 1.8 Å and modelling studies of its interaction with the tetra-haem cytochrome c3. J Biol Inorg Chem 2001; 6: 63-9.
    • (2001) J Biol Inorg Chem , vol.6 , pp. 63-69
    • Matias, P.M.1    Soares, C.M.2    Saraiva, L.M.3
  • 72
    • 66649106058 scopus 로고    scopus 로고
    • The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy
    • Stripp S, Sanganas O, Happe T, Haumann M. The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy. Biochemistry 2009; 48: 5042-9.
    • (2009) Biochemistry , vol.48 , pp. 5042-5049
    • Stripp, S.1    Sanganas, O.2    Happe, T.3    Haumann, M.4
  • 73
    • 35048826863 scopus 로고    scopus 로고
    • [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques
    • Lubitz W, Reijerse E, van Gastel M. [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques. Chem Rev 2007; 107: 4331-65.
    • (2007) Chem Rev , vol.107 , pp. 4331-4365
    • Lubitz, W.1    Reijerse, E.2    van Gastel, M.3
  • 74
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps JC, Volbeda A, Cavazza C, Nicolet Y. Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 2007; 107: 4273-303.
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 75
    • 48249113394 scopus 로고    scopus 로고
    • New frontiers in hydrogenase structure and biosynthesis
    • Posewitz MC, Mulder DW, Peters JW. New frontiers in hydrogenase structure and biosynthesis. Curr Chem Biol 2008; 2: 178-99.
    • (2008) Curr Chem Biol , vol.2 , pp. 178-199
    • Posewitz, M.C.1    Mulder, D.W.2    Peters, J.W.3
  • 76
    • 68949181269 scopus 로고    scopus 로고
    • Structure-function relationships of anaerobic gas-processing metalloenzymes
    • Fontecilla-Camps JC, Amara P, Cavazza C, Nicolet Y, Volbeda A. Structure-function relationships of anaerobic gas-processing metalloenzymes. Nature 2009; 460: 814-22.
    • (2009) Nature , vol.460 , pp. 814-822
    • Fontecilla-camps, J.C.1    Amara, P.2    Cavazza, C.3    Nicolet, Y.4    Volbeda, A.5
  • 77
    • 21244441201 scopus 로고    scopus 로고
    • Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site
    • Buhrke T, Lenz O, Krauss N, Friedrich B. Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site. J Biol Chem 2005; 280: 23791-6.
    • (2005) J Biol Chem , vol.280 , pp. 23791-23796
    • Buhrke, T.1    Lenz, O.2    Krauss, N.3    Friedrich, B.4
  • 78
    • 70350234815 scopus 로고    scopus 로고
    • Electrochemical kinetic investigations of the reactions of [FeFe]-hydrogenases with carbon monoxide and oxygen: comparing the importance of gas tunnels and active-site electronic/redox effects
    • Goldet G, Brandmayr C, Stripp ST, et al. Electrochemical kinetic investigations of the reactions of [FeFe]-hydrogenases with carbon monoxide and oxygen: comparing the importance of gas tunnels and active-site electronic/redox effects. J Am Chem Soc 2009; 131: 14979-89.
    • (2009) J Am Chem Soc , vol.131 , pp. 14979-14989
    • Goldet, G.1    Brandmayr, C.2    Stripp, S.T.3
  • 79
    • 0000030603 scopus 로고
    • Purification of hydrogenase from Chlamydomonas reinhardtii
    • Roessler PG, Lien S. Purification of hydrogenase from Chlamydomonas reinhardtii. Plant Physiol 1984; 75: 705-9.
    • (1984) Plant Physiol , vol.75 , pp. 705-709
    • Roessler, P.G.1    Lien, S.2
  • 80
  • 82
    • 0035794131 scopus 로고    scopus 로고
    • A novel type of iron hydrogenase in the green algae Scenodesmus obliguus is linked to the photosynthetic electron transport chain
    • Florin L, Tsokoglou A, Happe T. A novel type of iron hydrogenase in the green algae Scenodesmus obliguus is linked to the photosynthetic electron transport chain. J Biol Chem 2001; 276: 6125-32.
    • (2001) J Biol Chem , vol.276 , pp. 6125-6132
    • Florin, L.1    Tsokoglou, A.2    Happe, T.3
  • 83
    • 72749090095 scopus 로고    scopus 로고
    • How algae produce hydrogen-news from the photosynthetic hydrogenase
    • Stripp ST, Happe T. How algae produce hydrogen-news from the photosynthetic hydrogenase. Dalton Trans 2009; 45: 9960-9.
    • (2009) Dalton Trans , vol.45 , pp. 9960-9969
    • Stripp, S.T.1    Happe, T.2
  • 84
    • 73649099860 scopus 로고    scopus 로고
    • Characterization of the key step for light-driven hydrogen evolution in green algae
    • Winkler M, Kuhlgert S, Hippler M, Happe T. Characterization of the key step for light-driven hydrogen evolution in green algae. J Biol Chem 2009; 284: 36620-7.
    • (2009) J Biol Chem , vol.284 , pp. 36620-36627
    • Winkler, M.1    Kuhlgert, S.2    Hippler, M.3    Happe, T.4
  • 85
    • 0026761176 scopus 로고
    • Further characterization of the [Fe] hydrogenase from Desulfovibrio desulfuricans ATCC 7757
    • Hatchikian EC, Forget N, Fernandez VM, Williams R, Cammack R. Further characterization of the [Fe] hydrogenase from Desulfovibrio desulfuricans ATCC 7757. Eur J Biochem 1992; 209: 357-65.
    • (1992) Eur J Biochem , vol.209 , pp. 357-365
    • Hatchikian, E.C.1    Forget, N.2    Fernandez, V.M.3    Williams, R.4    Cammack, R.5
  • 86
    • 84882882968 scopus 로고    scopus 로고
    • Hydrogenases, hydrogen production and anoxia in Chlamydomonas reinhardtii
    • In: Stern D, Harris E, Eds. The Chlamydomonas Source Book. Amsterdam: Elsevier
    • Posewitz MC, Dubini A, Meuser J, Seibert M, Ghirardi ML. Hydrogenases, hydrogen production and anoxia in Chlamydomonas reinhardtii. In: Stern D, Harris E, Eds. The Chlamydomonas Source Book. Amsterdam: Elsevier 2008; pp. 217-55.
    • (2008) , pp. 217-255
    • Posewitz, M.C.1    Dubini, A.2    Meuser, J.3    Seibert, M.4    Ghirardi, M.L.5
  • 87
    • 0037715163 scopus 로고    scopus 로고
    • Expression of two [Fe]-hydrogenases in Chlamydomonas reinhardtii under anaerobic conditions
    • Forestier M, King P, Zhang L, et al. Expression of two [Fe]-hydrogenases in Chlamydomonas reinhardtii under anaerobic conditions. Eur J Biochem 2003; 270: 2750-8.
    • (2003) Eur J Biochem , vol.270 , pp. 2750-2758
    • Forestier, M.1    King, P.2    Zhang, L.3
  • 88
    • 0034669689 scopus 로고    scopus 로고
    • FTIR characterization of the active site of the Fe-hydrogenase from Desulfovibrio desulfuricans
    • De Lacey AL, Sradler C, Cavazza C, Hatchikian EC, Fernandez VM. FTIR characterization of the active site of the Fe-hydrogenase from Desulfovibrio desulfuricans. J Am Chem Soc 2000; 122: 11232-3.
    • (2000) J Am Chem Soc , vol.122 , pp. 11232-11233
    • De Lacey, A.L.1    Sradler, C.2    Cavazza, C.3    Hatchikian, E.C.4    Fernandez, V.M.5
  • 90
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • Nicolet Y, de Lacey AL, Vernède X, Fernandez VM, Hatchikian EC, Fontecilla-Camps JC. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J Am Chem Soc 2001; 123: 1596-601.
    • (2001) J Am Chem Soc , vol.123 , pp. 1596-1601
    • Nicolet, Y.1    De Lacey, A.L.2    Vernède, X.3    Fernandez, V.M.4    Hatchikian, E.C.5    Fontecilla-camps, J.C.6
  • 91
    • 0036523377 scopus 로고    scopus 로고
    • Hydrogenases: hydrogen-activating enzymes
    • Frey M. Hydrogenases: hydrogen-activating enzymes. Chembiochem 2002; 3: 153-60.
    • (2002) Chembiochem , vol.3 , pp. 153-160
    • Frey, M.1
  • 92
    • 14644393653 scopus 로고    scopus 로고
    • Identification of genes required for hydrogenase activity in Chlamydomonas reinhardtii
    • Posewitz MC, King PW, Smolinksi SL, et al. Identification of genes required for hydrogenase activity in Chlamydomonas reinhardtii. Biochem Soc Trans 2005; 33: 102-4.
    • (2005) Biochem Soc Trans , vol.33 , pp. 102-104
    • Posewitz, M.C.1    King, P.W.2    Smolinksi, S.L.3
  • 93
    • 0028865421 scopus 로고
    • Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool
    • Escoubas JM, Lomas M, LaRoche J, Falkowski PG. Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool. Proc Natl Acad Sci USA 1995; 92(22): 10237-41.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.22 , pp. 10237-10241
    • Escoubas, J.M.1    Lomas, M.2    LaRoche, J.3    Falkowski, P.G.4
  • 94
    • 0035965292 scopus 로고    scopus 로고
    • A novel mechanism of nuclear photosynthesis gene regulation by redox signals from the chloroplast during photosystem stoichiometry adjustment
    • Pfannschmidt T, Schutze K, Brost M, Oelmüller R. A novel mechanism of nuclear photosynthesis gene regulation by redox signals from the chloroplast during photosystem stoichiometry adjustment. J Biol Chem 2001; 276: 36125-30.
    • (2001) J Biol Chem , vol.276 , pp. 36125-36130
    • Pfannschmidt, T.1    Schutze, K.2    Brost, M.3    Oelmüller, R.4
  • 95
    • 24344440880 scopus 로고    scopus 로고
    • Finding gas diffusion pathways in proteins: Application to O2 and H2 transport in CpI [FeFe]-hydrogenase and the role of packing defects
    • Cohen J, Kim K, King P, Seibert M, Schulten K. Finding gas diffusion pathways in proteins: Application to O2 and H2 transport in CpI [FeFe]-hydrogenase and the role of packing defects. Structure 2005; 13: 1321-9.
    • (2005) Structure , vol.13 , pp. 1321-1329
    • Cohen, J.1    Kim, K.2    King, P.3    Seibert, M.4    Schulten, K.5
  • 96
    • 0019436382 scopus 로고
    • Comparative characterization of two distinct hydrogenases from Anabaena sp
    • Houchins JP, Burris RH. Comparative characterization of two distinct hydrogenases from Anabaena sp. strain 7120. J Bacteriol 1981; 146: 215-21.
    • (1981) strain 7120. J Bacteriol , vol.146 , pp. 215-221
    • Houchins, J.P.1    Burris, R.H.2
  • 99
    • 2142712975 scopus 로고    scopus 로고
    • Cyanobacterial type, heteropentameric, NAD+ reducing [NiFe] hydrogenase in the purple sulfur photosynthetic bacterium, Thiocapsa roseopersicina
    • Rákhely G, Kovács ÁT, Maróti G, et al. Cyanobacterial type, heteropentameric, NAD+ reducing [NiFe] hydrogenase in the purple sulfur photosynthetic bacterium, Thiocapsa roseopersicina. Appl Environ Microbiol 2004; 70: 722-8.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 722-728
    • Rákhely, G.1    Kovács, ÁT.2    Maróti, G.3
  • 100
    • 33845355867 scopus 로고    scopus 로고
    • Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module
    • Long M, Liu J, Chen Z, Bleijlevens B, RoseboomW, Albracht SP. Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module. J Biol Inorg Chem 2007; 12: 62-78.
    • (2007) J Biol Inorg Chem , vol.12 , pp. 62-78
    • Long, M.1    Liu, J.2    Chen, Z.3    Bleijlevens, B.4    Roseboom, W.5    Albracht, S.P.6
  • 101
    • 0028883622 scopus 로고
    • Molecular biological analysis of a bidirectional hydrogenase from cyanobacteria
    • Schmitz O, Boison G, Hilscher R, et al. Molecular biological analysis of a bidirectional hydrogenase from cyanobacteria. Eur J Biochem 1995; 233: 266-76.
    • (1995) Eur J Biochem , vol.233 , pp. 266-276
    • Schmitz, O.1    Boison, G.2    Hilscher, R.3
  • 103
    • 0030607245 scopus 로고    scopus 로고
    • Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans
    • Boison G, Schmitz O, Mikheeva L, Shestakov S, Bothe H. Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans. FEBS Lett 1996; 394: 153-8.
    • (1996) FEBS Lett , vol.394 , pp. 153-158
    • Boison, G.1    Schmitz, O.2    Mikheeva, L.3    Shestakov, S.4    Bothe, H.5
  • 104
    • 0037057140 scopus 로고    scopus 로고
    • Identification of hox genes and analysis of their transcription in the unicellular cyanobacterium Gloeocapsa alpicola CALU 743 growing under nitrate-limiting conditions
    • Sheremetieva ME, Troshina OY, Serebryakova LT, Lindblad P. Identification of hox genes and analysis of their transcription in the unicellular cyanobacterium Gloeocapsa alpicola CALU 743 growing under nitrate-limiting conditions. FEMS Microbiol Lett 2002; 214: 229-33.
    • (2002) FEMS Microbiol Lett , vol.214 , pp. 229-233
    • Sheremetieva, M.E.1    Troshina, O.Y.2    Serebryakova, L.T.3    Lindblad, P.4
  • 105
    • 0037156874 scopus 로고    scopus 로고
    • HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria
    • Schmitz O, Boison G, Salzmann H, et al. HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria. BBA-Bioenergetics 2002; 1554: 66-74.
    • (2002) BBA-Bioenergetics , vol.1554 , pp. 66-74
    • Schmitz, O.1    Boison, G.2    Salzmann, H.3
  • 106
    • 0028009865 scopus 로고
    • Purification and characterization of the membrane-bound hydrogenase from from Methanosarcina barkeri MS
    • Kemner J, Zeikus JG. Purification and characterization of the membrane-bound hydrogenase from from Methanosarcina barkeri MS. Arch Microbiol 1994; 161: 47-54.
    • (1994) Arch Microbiol , vol.161 , pp. 47-54
    • Kemner, J.1    Zeikus, J.G.2
  • 107
    • 0036275140 scopus 로고    scopus 로고
    • Characterization of the oxygen tolerance of a hydrogenase linked to a carbon monoxide oxidation pathway in Rubrivivax gelatinosus
    • Maness PC, Smolinski S, Dillon AC, Heben MJ, Weaver PF. Characterization of the oxygen tolerance of a hydrogenase linked to a carbon monoxide oxidation pathway in Rubrivivax gelatinosus. Appl Environ Microbiol 2002; 68: 2633-6.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 2633-2636
    • Maness, P.C.1    Smolinski, S.2    Dillon, A.C.3    Heben, M.J.4    Weaver, P.F.5
  • 108
    • 0036135161 scopus 로고    scopus 로고
    • Transcriptional regulation of Nostoc hydrogenases: effects of oxygen, hydrogen, and nickel
    • Axelsson R, Lindblad P. Transcriptional regulation of Nostoc hydrogenases: effects of oxygen, hydrogen, and nickel. Appl Environ Microbiol 2002; 68: 444-7.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 444-447
    • Axelsson, R.1    Lindblad, P.2
  • 110
    • 72749104137 scopus 로고    scopus 로고
    • Transcriptional regulation of the cyanobacterial bidirectional Hox-hydrogenase
    • Oliveira P, Lindblad P. Transcriptional regulation of the cyanobacterial bidirectional Hox-hydrogenase. Dalton Trans 2009; 7: 9990-6.
    • (2009) Dalton Trans , vol.7 , pp. 9990-9996
    • Oliveira, P.1    Lindblad, P.2
  • 111
    • 67349247430 scopus 로고    scopus 로고
    • Transcriptional regulation of the bidirectional hydrogenase in the cyanobacterium Synechocystis 6803
    • Kiss É, Kós PB, Vass I. Transcriptional regulation of the bidirectional hydrogenase in the cyanobacterium Synechocystis 6803. J Biotechnol 2009; 142: 31-7.
    • (2009) J Biotechnol , vol.142 , pp. 31-37
    • É, K.1    Kós, P.B.2    Vass, I.3
  • 113
    • 33745662408 scopus 로고    scopus 로고
    • Production and scavenging of reactive oxygen species in chloroplasts and their function
    • Asada K. Production and scavenging of reactive oxygen species in chloroplasts and their function. 2006 141: 391-6.
    • (2006) , vol.141 , pp. 391-396
    • Asada, K.1
  • 114
    • 0001219252 scopus 로고    scopus 로고
    • Structure-function relationships of alternative nitrogenases
    • Eady RR. Structure-function relationships of alternative nitrogenases. Chem Rev 1996; 96: 3013-30.
    • (1996) Chem Rev , vol.96 , pp. 3013-3030
    • Eady, R.R.1
  • 115
    • 34247506549 scopus 로고    scopus 로고
    • Nitrogen fixation in heterocyst-forming cyanobacteria. Chapter 5
    • In: Klipp W, Masepohl B, Gallon JR, Newton WE, Eds. Genetics and regulation of nitrogen fixing bacteria. Netherlands: Kluwer Academic Publishers
    • Thiel T. Nitrogen fixation in heterocyst-forming cyanobacteria. Chapter 5. In: Klipp W, Masepohl B, Gallon JR, Newton WE, Eds. Genetics and regulation of nitrogen fixing bacteria. Netherlands: Kluwer Academic Publishers 2004; pp. 73-110.
    • (2004) , pp. 73-110
    • Thiel, T.1
  • 116
    • 0000912550 scopus 로고    scopus 로고
    • Hydrogen photoproduction by three different nitrogenases in whole cells of Anabaena variabilis and the dependence on pH
    • Tsygankov AS, Serebryakova LT, Sveshnikov DA, Rao KK, Gogotov. Hydrogen photoproduction by three different nitrogenases in whole cells of Anabaena variabilis and the dependence on pH. Int J Hydrogen Energy 1997; 22: 859-67.
    • (1997) Int J Hydrogen Energy , vol.22 , pp. 859-867
    • Tsygankov, A.S.1    Serebryakova, L.T.2    Sveshnikov, D.A.3    Gogotov, R.K.K.4
  • 118
    • 70349138077 scopus 로고    scopus 로고
    • Synthesis, structures, and electronic properties of [8Fe-7S] cluster complexes modeling the nitrogenase P-cluster
    • Ohki Y, Imada M, Murata A, et al. Synthesis, structures, and electronic properties of [8Fe-7S] cluster complexes modeling the nitrogenase P-cluster. J Am Chem Soc 2009; 131: 13168-78.
    • (2009) J Am Chem Soc , vol.131 , pp. 13168-13178
    • Ohki, Y.1    Imada, M.2    Murata, A.3
  • 119
    • 70349576592 scopus 로고    scopus 로고
    • A substrate channel in the nitrogenase MoFe protein
    • Barney BM, Yurth MG, Dos Santos PC, et al. A substrate channel in the nitrogenase MoFe protein. J Biol Inorg Chem 2009; 14: 1015-22.
    • (2009) J Biol Inorg Chem , vol.14 , pp. 1015-1022
    • Barney, B.M.1    Yurth, M.G.2    Santos, P.C.3
  • 120
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess BK, Lowe DJ. Mechanism of molybdenum nitrogenase. Chem Rev 1996; 96: 2983-3012.
    • (1996) Chem Rev , vol.96 , pp. 2983-3012
    • Burgess, B.K.1    Lowe, D.J.2
  • 121
    • 0035340589 scopus 로고    scopus 로고
    • Controlled protonation of iron-molybdenum cofactor by nitrogenase: a structural and theoretical analysis
    • Durrant MC. Controlled protonation of iron-molybdenum cofactor by nitrogenase: a structural and theoretical analysis. Biochem J 2001; 355: 569-76.
    • (2001) Biochem J , vol.355 , pp. 569-576
    • Durrant, M.C.1
  • 123
    • 84884454074 scopus 로고    scopus 로고
    • The role of Nif proteins in nitrogenase maturation
    • In: Dakora FD, Chimphango SBM, Valentine AJ, Elmerich C, Newton WE, Eds. Biological nitrogen fixation: towards poverty alleviation through sustainable agriculture. Cape Town, South Africa: Springer
    • Rubio LM, Hernandez JA, Soboh B, et al. The role of Nif proteins in nitrogenase maturation. In: Dakora FD, Chimphango SBM, Valentine AJ, Elmerich C, Newton WE, Eds. Biological nitrogen fixation: towards poverty alleviation through sustainable agriculture. Cape Town, South Africa: Springer 2008; 325-8.
    • (2008) , pp. 325-328
    • Rubio, L.M.1    Hernandez, J.A.2    Soboh, B.3
  • 124
    • 68949107281 scopus 로고    scopus 로고
    • Molybdenum cofactors, enzymes and pathways
    • Schwarz G, Mendel RR, Ribbe MW. Molybdenum cofactors, enzymes and pathways. Nature 2009; 460: 839-47.
    • (2009) Nature , vol.460 , pp. 839-847
    • Schwarz, G.1    Mendel, R.R.2    Ribbe, M.W.3
  • 125
    • 0030611894 scopus 로고    scopus 로고
    • N2 fixation by Streptomyces thermoautotrophicus involves a molybdenum-dinitrogenase and a manganese-superoxide oxidoreductase that couple N2 reduction to the oxidation of superoxide produced from O2 by a molybdenum-CO dehydrogenase
    • Ribbe M, Gadkari D, Meyer O. N2 fixation by Streptomyces thermoautotrophicus involves a molybdenum-dinitrogenase and a manganese-superoxide oxidoreductase that couple N2 reduction to the oxidation of superoxide produced from O2 by a molybdenum-CO dehydrogenase. J Biol Chem 1997; 272: 26627-33.
    • (1997) J Biol Chem , vol.272 , pp. 26627-26633
    • Ribbe, M.1    Gadkari, D.2    Meyer, O.3
  • 126
    • 0000801645 scopus 로고
    • Effects of growth irradiance and nitrogen limitation on photosynthetic energy conversion in Photosystem II
    • Kolber Z, Zehr J, Falkowski P. Effects of growth irradiance and nitrogen limitation on photosynthetic energy conversion in Photosystem II. Plant Physiol 1988; 88: 923-9.
    • (1988) Plant Physiol , vol.88 , pp. 923-929
    • Kolber, Z.1    Zehr, J.2    Falkowski, P.3
  • 127
    • 0032068061 scopus 로고    scopus 로고
    • The effects of phosphorus and sulfur deprivation on photosynthetic electron transport in Chlamydomonas reinhardtii
    • Wykoff DD, Davies JP, Melis A, Grossman A. The effects of phosphorus and sulfur deprivation on photosynthetic electron transport in Chlamydomonas reinhardtii. Plant Physiol 1998; 117: 129-39.
    • (1998) Plant Physiol , vol.117 , pp. 129-139
    • Wykoff, D.D.1    Davies, J.P.2    Melis, A.3    Grossman, A.4
  • 128
    • 6344221872 scopus 로고    scopus 로고
    • Insights into the survival of Chlamydomonas reinhardtii during sulfur starvation based on microarray analysis of gene expression
    • Zhang Z, Shrager J, Jain M, Chang CW, Vallon O, Grossman A. Insights into the survival of Chlamydomonas reinhardtii during sulfur starvation based on microarray analysis of gene expression. Eukaryot Cell 2004; 3: 1331-48.
    • (2004) Eukaryot Cell , vol.3 , pp. 1331-1348
    • Zhang, Z.1    Shrager, J.2    Jain, M.3    Chang, C.W.4    Vallon, O.5    Grossman, A.6
  • 129
    • 55749106801 scopus 로고    scopus 로고
    • Transcriptome for photobiological hydrogen production induced by sulfur deprivation in the green alga Chlamydomonas reinhardtii
    • Nguyen AV, Thomas-Hall SR, Malnoë A, et al. Transcriptome for photobiological hydrogen production induced by sulfur deprivation in the green alga Chlamydomonas reinhardtii. Eukaryot Cell 2008; 7: 1965-79.
    • (2008) Eukaryot Cell , vol.7 , pp. 1965-1979
    • Nguyen, A.V.1    Thomas-hall, S.R.2    Malnoë, A.3
  • 131
    • 33748750982 scopus 로고    scopus 로고
    • Effects of sulfur limitation on the PS II functioning in Chlamydomonas reinhardtii as probed by the chlorophyll a fluorescence
    • Antal TK, Volgusheva AA, Kukarskih GP, Bulychev AA, Krendeleva TE, Rubin AB. Effects of sulfur limitation on the PS II functioning in Chlamydomonas reinhardtii as probed by the chlorophyll a fluorescence. Physiol Plantarum 2006; 128: 360-7.
    • (2006) Physiol Plantarum , vol.128 , pp. 360-367
    • Antal, T.K.1    Volgusheva, A.A.2    Kukarskih, G.P.3    Bulychev, A.A.4    Krendeleva, T.E.5    Rubin, A.B.6
  • 132
    • 0010323681 scopus 로고    scopus 로고
    • Two-phase photobiological algal H2-production system. Proceedings of the 2000 DOE Hydrogen Program Review
    • NREL/CP-570-28890
    • Ghirardi ML, Kosourov SN, Tsygankov AA, Seibert M. Two-phase photobiological algal H2-production system. Proceedings of the 2000 DOE Hydrogen Program Review. NREL/CP-570-28890.
    • Ghirardi, M.L.1    Kosourov, S.N.2    Tsygankov, A.A.3    Seibert, M.4
  • 133
    • 0345059199 scopus 로고    scopus 로고
    • The dependence of algal H2 production on Photosystem II and O2 consumption activities in sulfur deprived Chlamydomonas reinhardtii cells
    • Antal TK, Krendeleva TE, Laurinavichene TV, et al. The dependence of algal H2 production on Photosystem II and O2 consumption activities in sulfur deprived Chlamydomonas reinhardtii cells. BBA-Bioenergetics 2003; 1607: 153-60.
    • (2003) BBA-Bioenergetics , vol.1607 , pp. 153-160
    • Antal, T.K.1    Krendeleva, T.E.2    Laurinavichene, T.V.3
  • 134
    • 21744446408 scopus 로고    scopus 로고
    • Inhibitor studies on non-photochemical plastoquinone reduction and H2 photoproduction in Chlamydomonas reinhardtii
    • Mus F, Cournac L, Cardettini V, Caruana A, Peltier G. Inhibitor studies on non-photochemical plastoquinone reduction and H2 photoproduction in Chlamydomonas reinhardtii. BBA-Bioenergetics 2005; 1708: 322-32.
    • (2005) BBA-Bioenergetics , vol.1708 , pp. 322-332
    • Mus, F.1    Cournac, L.2    Cardettini, V.3    Caruana, A.4    Peltier, G.5
  • 135
    • 58149483399 scopus 로고    scopus 로고
    • A type II NAD(P)H dehydrogenase mediates light-independent plastoquinone reduction in the chloroplast of Chlamydomonas
    • Jans F, Mignolet E, Houyoux P-A, et al. A type II NAD(P)H dehydrogenase mediates light-independent plastoquinone reduction in the chloroplast of Chlamydomonas. Proc Natl Acad Sci USA 2008; 105: 20546-51.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20546-20551
    • Jans, F.1    Mignolet, E.2    Houyoux, P.-A.3
  • 136
    • 63249099166 scopus 로고    scopus 로고
    • Characterization of Nda2, a plastoquinone-reducing type II NAD(P)H dehydrogenase in Chlamydomonas chloroplasts
    • Desplats C, Mus F, Cuine S, Billon E, Cournac L, Peltier G. Characterization of Nda2, a plastoquinone-reducing type II NAD(P)H dehydrogenase in Chlamydomonas chloroplasts. J Biol Chem 2009; 284: 4148-57.
    • (2009) J Biol Chem , vol.284 , pp. 4148-4157
    • Desplats, C.1    Mus, F.2    Cuine, S.3    Billon, E.4    Cournac, L.5    Peltier, G.6
  • 137
    • 71849095917 scopus 로고    scopus 로고
    • Relationships between H2 photoproduction and different electron transport pathways in sulfur-deprived Chlamydomonas reinhardtii
    • Antal TK, Volgusheva AA, Kukarskih GP, Krendeleva TE, Rubin AB. Relationships between H2 photoproduction and different electron transport pathways in sulfur-deprived Chlamydomonas reinhardtii. Int J Hydrogen Energy 2009; 34: 9087-94.
    • (2009) Int J Hydrogen Energy , vol.34 , pp. 9087-9094
    • Antal, T.K.1    Volgusheva, A.A.2    Kukarskih, G.P.3    Krendeleva, T.E.4    Rubin, A.B.5
  • 138
    • 0004127469 scopus 로고    scopus 로고
    • Regulation of Photosynthesis
    • Dordrecht: Kluwer Academic Publishers
    • Aro EM, Andersson B, Eds. Regulation of Photosynthesis. Dordrecht: Kluwer Academic Publishers, 2001.
    • (2001)
    • Aro, E.M.1    Andersson, B.2
  • 139
    • 0035522804 scopus 로고    scopus 로고
    • The relationship between photosystem 2 activity and hydrogen production in sulfur deprived Chlamydomonas reinhardtii cells
    • Antal TK, Krendeleva TE, Laurinavichene TV, et al. The relationship between photosystem 2 activity and hydrogen production in sulfur deprived Chlamydomonas reinhardtii cells. Dokl Biochem Biophys 2001; 381: 371-4.
    • (2001) Dokl Biochem Biophys , vol.381 , pp. 371-374
    • Antal, T.K.1    Krendeleva, T.E.2    Laurinavichene, T.V.3
  • 140
    • 16644388467 scopus 로고    scopus 로고
    • The photochemical activity of photosystem II in sulfur-deprived Chlamydomonas reinhardtii cells depends on the redox state of the quinone pool during the transition to anaerobiosis
    • Antal TK, Krendeleva TE, Rubin AB. The photochemical activity of photosystem II in sulfur-deprived Chlamydomonas reinhardtii cells depends on the redox state of the quinone pool during the transition to anaerobiosis. Biofizika 2004; 49: 499-505.
    • (2004) Biofizika , vol.49 , pp. 499-505
    • Antal, T.K.1    Krendeleva, T.E.2    Rubin, A.B.3
  • 141
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • Allen JF, Bennet J, Steinback KE, Arntzen CJ. Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature 1981; 291: 25-9.
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, J.F.1    Bennet, J.2    Steinback, K.E.3    Arntzen, C.J.4
  • 142
    • 33847340991 scopus 로고    scopus 로고
    • A comparison of hydrogen photoproduction by sulfur-deprived Chlamydomonas reinhardtii under different growth conditions
    • Kosourov S, Patrusheva E, Ghirardi ML, Seibert M, Tsygankov A. A comparison of hydrogen photoproduction by sulfur-deprived Chlamydomonas reinhardtii under different growth conditions. J Biotechnol 2007; 128: 776-87.
    • (2007) J Biotechnol , vol.128 , pp. 776-787
    • Kosourov, S.1    Patrusheva, E.2    Ghirardi, M.L.3    Seibert, M.4    Tsygankov, A.5
  • 145
    • 0037330899 scopus 로고    scopus 로고
    • Effects of extracellular pH on the metabolic pathways in sulfur-deprived, H2-producing Chlamydomonas reinhardtii cultures
    • Kosourov S, Seibert MS, Ghirardi ML. Effects of extracellular pH on the metabolic pathways in sulfur-deprived, H2-producing Chlamydomonas reinhardtii cultures. Plant Cell Physiol 2003 44: 146-55.
    • (2003) Plant Cell Physiol , vol.44 , pp. 146-155
    • Kosourov, S.1    Seibert, M.S.2    Ghirardi, M.L.3
  • 146
    • 40949128266 scopus 로고    scopus 로고
    • Hydrogen production by Chlamydomonas reinhardtii: an elaborate interplay of electron sources and sinks
    • Hemschemeier A, Fouchard S, Cournac L, Peltier G, Happe T. Hydrogen production by Chlamydomonas reinhardtii: an elaborate interplay of electron sources and sinks. Planta 2008; 227: 397-407.
    • (2008) Planta , vol.227 , pp. 397-407
    • Hemschemeier, A.1    Fouchard, S.2    Cournac, L.3    Peltier, G.4    Happe, T.5
  • 147
    • 4043114949 scopus 로고    scopus 로고
    • Hydrogen photoproduction is attenuated by disruption of an isoamylase gene in Chlamydomonas reinhardtii
    • Posewitz MC, Smolinski SL, Kanakagiri S, Melis A, Seibert M, Ghirardi ML. Hydrogen photoproduction is attenuated by disruption of an isoamylase gene in Chlamydomonas reinhardtii. Plant Cell 2004; 16: 2151-63.
    • (2004) Plant Cell , vol.16 , pp. 2151-2163
    • Posewitz, M.C.1    Smolinski, S.L.2    Kanakagiri, S.3    Melis, A.4    Seibert, M.5    Ghirardi, M.L.6
  • 148
    • 0036208158 scopus 로고    scopus 로고
    • Involvement of state transition in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii
    • Finazzi G, Rappaport F, Furia A, Fleischmann M. Involvement of state transition in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii. EMBO Rep 2002; 3: 280-5.
    • (2002) EMBO Rep , vol.3 , pp. 280-285
    • Finazzi, G.1    Rappaport, F.2    Furia, A.3    Fleischmann, M.4
  • 149
    • 26644462167 scopus 로고    scopus 로고
    • Improved photobiological H2 production in engineered green algal cells
    • Kruse O, Rupprecht J, Bader K, et al . Improved photobiological H2 production in engineered green algal cells. J Biol Chem 2005; 280: 34170-7.
    • (2005) J Biol Chem , vol.280 , pp. 34170-34177
    • Kruse, O.1    Rupprecht, J.2    Bader, K.3
  • 150
    • 34547764830 scopus 로고    scopus 로고
    • Photosynthetic biomass and H2 production by green algae: from bioengineering to bioreactor scale-up
    • Hankamer B, Lehr F, Rupprecht J, Mussgnug JH, Posten C, Kruse O. Photosynthetic biomass and H2 production by green algae: from bioengineering to bioreactor scale-up. Physiol Plantarum 2007 131: 10-21.
    • (2007) Physiol Plantarum , vol.131 , pp. 10-21
    • Hankamer, B.1    Lehr, F.2    Rupprecht, J.3    Mussgnug, J.H.4    Posten, C.5    Kruse, O.6
  • 151
    • 38549093143 scopus 로고    scopus 로고
    • Hydrogen fuel production by transgenic microalgae
    • Melis A, Seibert M, Ghirardi ML. Hydrogen fuel production by transgenic microalgae. Adv Exp Med Biol 2007; 616: 110-21.
    • (2007) Adv Exp Med Biol , vol.616 , pp. 110-121
    • Melis, A.1    Seibert, M.2    Ghirardi, M.L.3
  • 152
    • 67349093990 scopus 로고    scopus 로고
    • From systems biology to fuel - Chlamydomonas reinhardtii as a model for a systems biology approach to improve biohydrogen production
    • Rupprecht J. From systems biology to fuel - Chlamydomonas reinhardtii as a model for a systems biology approach to improve biohydrogen production. J Biotechnol 2009; 142: 10-20.
    • (2009) J Biotechnol , vol.142 , pp. 10-20
    • Rupprecht, J.1
  • 153
    • 4644293940 scopus 로고    scopus 로고
    • The effect of light intensity on hydrogen production by sulfur-deprived Chlamydomonas reinhardtii
    • Laurinavichene TV, Tolstygina IV, Tsygankov AA. The effect of light intensity on hydrogen production by sulfur-deprived Chlamydomonas reinhardtii. J Biotechnol 2004; 114: 143-51.
    • (2004) J Biotechnol , vol.114 , pp. 143-151
    • Laurinavichene, T.V.1    Tolstygina, I.V.2    Tsygankov, A.A.3
  • 154
    • 33746906637 scopus 로고    scopus 로고
    • Enhanced hydrogen production by controlling light intensity in sulfur-deprived Chlamydomonas reinhardtii culture
    • Kim JP, Chang DK, Tai HP, Mi SK, Sang JS. Enhanced hydrogen production by controlling light intensity in sulfur-deprived Chlamydomonas reinhardtii culture. Int J Hydrogen Energy 2006; 31: 1585-90.
    • (2006) Int J Hydrogen Energy , vol.31 , pp. 1585-1590
    • Kim, J.P.1    Chang, D.K.2    Tai, H.P.3    Mi, S.K.4    Sang, J.S.5
  • 155
    • 69249095798 scopus 로고    scopus 로고
    • Interplay between light intensity, chlorophyll concentration and culture mixing on the hydrogen production in sulfur-deprived Chlamydomonas reinhardtii cultures grown in laboratory photobioreactors
    • Giannelli L, Scoma A, Torzillo G. Interplay between light intensity, chlorophyll concentration and culture mixing on the hydrogen production in sulfur-deprived Chlamydomonas reinhardtii cultures grown in laboratory photobioreactors. Biotechnol Bioeng 2009; 104: 76-90.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 76-90
    • Giannelli, L.1    Scoma, A.2    Torzillo, G.3
  • 156
    • 0036836413 scopus 로고    scopus 로고
    • Hydrogen photoproduction under continuous illumination by sulfur-deprived, synchronous Chlamydomonas reinhardtii cultures
    • Tsygankov A, Kosourov S, Seibert M, Ghirardi ML. Hydrogen photoproduction under continuous illumination by sulfur-deprived, synchronous Chlamydomonas reinhardtii cultures. Int J Hydrogen Energy 2002; 27: 1239-44.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1239-1244
    • Tsygankov, A.1    Kosourov, S.2    Seibert, M.3    Ghirardi, M.L.4
  • 157
    • 41549096266 scopus 로고    scopus 로고
    • Prolongation of H2 photoproduction by immobilized, sulfur-limited Chlamydomonas reinhardtii cultures
    • Laurinavichene TV, Kosourov SN, Ghirardi ML, Seibert M, Tsygankov AA. Prolongation of H2 photoproduction by immobilized, sulfur-limited Chlamydomonas reinhardtii cultures. J Biotechnol 2008; 134: 275-7.
    • (2008) J Biotechnol , vol.134 , pp. 275-277
    • Laurinavichene, T.V.1    Kosourov, S.N.2    Ghirardi, M.L.3    Seibert, M.4    Tsygankov, A.A.5
  • 158
    • 58149218801 scopus 로고    scopus 로고
    • Hydrogen photoproduction by nutrient-deprived Chlamydomonas reinhardtii cells immobilized within thin alginate films under aerobic and anaerobic conditions
    • Kosourov S, Seibert M. Hydrogen photoproduction by nutrient-deprived Chlamydomonas reinhardtii cells immobilized within thin alginate films under aerobic and anaerobic conditions. Biotechnol Bioeng 2008; 102: 50-8.
    • (2008) Biotechnol Bioeng , vol.102 , pp. 50-58
    • Kosourov, S.1    Seibert, M.2
  • 159
    • 18844380864 scopus 로고    scopus 로고
    • Continuous hydrogen photoproduction by Chlamydomonas reinhardtii using a novel two-stage, sulfate-limited chemostat system
    • Fedorov AS, Kosourov S, Ghirardi ML, Seibert M. Continuous hydrogen photoproduction by Chlamydomonas reinhardtii using a novel two-stage, sulfate-limited chemostat system. Appl Biochem Biotechnol 2005; 121: 403-12.
    • (2005) Appl Biochem Biotechnol , vol.121 , pp. 403-412
    • Fedorov, A.S.1    Kosourov, S.2    Ghirardi, M.L.3    Seibert, M.4
  • 160
    • 69349089915 scopus 로고    scopus 로고
    • Photo-bioproduction of hydrogen by Chlamydomonas reinhardtii using a semi-continuous process regime
    • Oncel S, Vardar-Sukan F. Photo-bioproduction of hydrogen by Chlamydomonas reinhardtii using a semi-continuous process regime. Int J Hydrogen Energy 2009; 34: 7592-602.
    • (2009) Int J Hydrogen Energy , vol.34 , pp. 7592-7602
    • Oncel, S.1    Vardar-sukan, F.2
  • 161
    • 65949117066 scopus 로고    scopus 로고
    • Increased hydrogen photoproduction by means of a sulfur-deprived Chlamydomonas reinhardtii D1 protein mutant
    • Torzillo G, Scoma A, Faraloni C, Ena A, Johanningmeier U. Increased hydrogen photoproduction by means of a sulfur-deprived Chlamydomonas reinhardtii D1 protein mutant. Int J Hydrogen Energy 2009; 34: 4529-36.
    • (2009) Int J Hydrogen Energy , vol.34 , pp. 4529-4536
    • Torzillo, G.1    Scoma, A.2    Faraloni, C.3    Ena, A.4    Johanningmeier, U.5
  • 162
    • 23444454349 scopus 로고    scopus 로고
    • Role of SulP, a nuclear-encoded chloroplast sulfate permease, in sulfate transport and H2 evolution in Chlamydomonas reinhardtii
    • Chen HC, Newton AJ, Melis A. Role of SulP, a nuclear-encoded chloroplast sulfate permease, in sulfate transport and H2 evolution in Chlamydomonas reinhardtii. Photosynth Res 2005; 84: 289-96.
    • (2005) Photosynth Res , vol.84 , pp. 289-296
    • Chen, H.C.1    Newton, A.J.2    Melis, A.3
  • 163
    • 26844473317 scopus 로고    scopus 로고
    • Autotrophic and mixotrophic hydrogen photoproduction in sulfur-deprived Chlamydomonas cells
    • Fouchard S, Hemschemeier A, Caruana A, et al. Autotrophic and mixotrophic hydrogen photoproduction in sulfur-deprived Chlamydomonas cells. Appl Environ Microbiol 2005; 71: 6199-205.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 6199-6205
    • Fouchard, S.1    Hemschemeier, A.2    Caruana, A.3
  • 165
    • 60549098776 scopus 로고    scopus 로고
    • Hydrogen production by photoautotrophic sulfur-deprived Chlamydomonas reinhardtii pre-grown and incubated under high light
    • Tolstygina IV, Antal TK, Kosourov SN, Krendeleva TE, Rubin AB, Tsygankov AA. Hydrogen production by photoautotrophic sulfur-deprived Chlamydomonas reinhardtii pre-grown and incubated under high light. Biotechnol Bioeng 2009; 102: 1055-61.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1055-1061
    • Tolstygina, I.V.1    Antal, T.K.2    Kosourov, S.N.3    Krendeleva, T.E.4    Rubin, A.B.5    Tsygankov, A.A.6
  • 166
    • 0344534171 scopus 로고    scopus 로고
    • Stably sustained hydrogen production by biophotolysis in natural day/night cycle
    • Miura Y, Akano T, Fukatsu K, et al. Stably sustained hydrogen production by biophotolysis in natural day/night cycle. Energ Convers Manage 1997; 38: S533-7.
    • (1997) Energ Convers Manage , vol.38
    • Miura, Y.1    Akano, T.2    Fukatsu, K.3
  • 167
    • 0031049012 scopus 로고
    • Fermentative metabolism to produce hydrogen gas and organic compounds in a cyanobacterium, Spirulina platensis
    • Aoyama K, Uemura I, Miyake J, Asada Y. Fermentative metabolism to produce hydrogen gas and organic compounds in a cyanobacterium, Spirulina platensis. J Ferment Bioeng 1987; 83: 17-26.
    • (1987) J Ferment Bioeng , vol.83 , pp. 17-26
    • Aoyama, K.1    Uemura, I.2    Miyake, J.3    Asada, Y.4
  • 168
    • 0036836356 scopus 로고    scopus 로고
    • Production of H2 by the unicellular cyanobacterium Gloeocapsa alpicola CALU 743 during fermentation
    • Troshina O, Serebryakova L, Sheremetieva M, Lindberg P. Production of H2 by the unicellular cyanobacterium Gloeocapsa alpicola CALU 743 during fermentation. Int J Hydrogen Energy 2002; 27: 1283-9.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1283-1289
    • Troshina, O.1    Serebryakova, L.2    Sheremetieva, M.3    Lindberg, P.4
  • 172
    • 55049127127 scopus 로고    scopus 로고
    • Optimization of media nutrient composition for increased photofermentative hydrogen production by Synechocystis sp
    • Burrows EH, Chaplen FWR, Ely RL. Optimization of media nutrient composition for increased photofermentative hydrogen production by Synechocystis sp. PCC 6803. Int J Hydrogen Energy 2008; 33: 6092-9.
    • (2008) PCC 6803. Int J Hydrogen Energy , vol.33 , pp. 6092-6099
    • Burrows, E.H.1    Chaplen, F.W.R.2    Ely, R.L.3
  • 173
    • 35348893751 scopus 로고    scopus 로고
    • Two-stage system for hydrogen production by immobilized cyanobacterium Gloeocapsa alpicola CALU 743
    • Serebryakova LT, Tsygankov AA. Two-stage system for hydrogen production by immobilized cyanobacterium Gloeocapsa alpicola CALU 743. Biotechnol Prog 2007; 23: 1106-10.
    • (2007) Biotechnol Prog , vol.23 , pp. 1106-1110
    • Serebryakova, L.T.1    Tsygankov, A.A.2
  • 174
    • 70349114195 scopus 로고    scopus 로고
    • Characteristics of hydrogen production by immobilized cyanobacterium Microcystis aeruginosa through cycles of photosynthesis and anaerobic incubation
    • Rashid N, Song W, Park J, Jin H-F, Lee K. Characteristics of hydrogen production by immobilized cyanobacterium Microcystis aeruginosa through cycles of photosynthesis and anaerobic incubation. J Ind Eng Chem 2009; 15: 498-503.
    • (2009) J Ind Eng Chem , vol.15 , pp. 498-503
    • Rashid, N.1    Song, W.2    Park, J.3    Jin, H.-F.4    Lee, K.5
  • 175
    • 33751534724 scopus 로고    scopus 로고
    • Genetic control of hydrogen metabolism in cyanobacteria
    • Shestakov SV, Mikheeva LE. Genetic control of hydrogen metabolism in cyanobacteria. Russ J Genet 2006; 42: 1272-84.
    • (2006) Russ J Genet , vol.42 , pp. 1272-1284
    • Shestakov, S.V.1    Mikheeva, L.E.2
  • 176
    • 34249687026 scopus 로고    scopus 로고
    • Nitrogen-fixing cyanobacteria: A review
    • Tsygankov A. Nitrogen-fixing cyanobacteria: A review. Appl Biochem Microbiol 2007; 43: 250-9.
    • (2007) Appl Biochem Microbiol , vol.43 , pp. 250-259
    • Tsygankov, A.1
  • 177
    • 0036215515 scopus 로고    scopus 로고
    • Disruption of the uptake hydrogenase gene, but not of the bidirectional hydrogenase gene, leads to enhanced photobiological hydrogen production by the nitrogen-fixing cyanobacterium Anabaena sp
    • Masukawa H, Mochimaru M, Sakurai H. Disruption of the uptake hydrogenase gene, but not of the bidirectional hydrogenase gene, leads to enhanced photobiological hydrogen production by the nitrogen-fixing cyanobacterium Anabaena sp. Appl Microbiol Biotechnol 2002; 58: 618-24.
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 618-624
    • Masukawa, H.1    Mochimaru, M.2    Sakurai, H.3
  • 178
    • 0036836351 scopus 로고    scopus 로고
    • A hydrogen-producing, hydrogenase-free mutant strain of Nostoc punctiforme ATCC 29133
    • Lindberg P, Schütz K, Happe T, Lindblad P. A hydrogen-producing, hydrogenase-free mutant strain of Nostoc punctiforme ATCC 29133. Int J Hydrogen Energy 2002; 27: 1291-6.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1291-1296
    • Lindberg, P.1    Schütz, K.2    Happe, T.3    Lindblad, P.4
  • 180
    • 76349116490 scopus 로고    scopus 로고
    • Hydrogen production in nitrogenase mutants in Anabaena variabilis
    • Weyman PD, Pratte B, Thiel T. Hydrogen production in nitrogenase mutants in Anabaena variabilis. FEMS Microbiol Lett 2010; 304: 55-61.
    • (2010) FEMS Microbiol Lett , vol.304 , pp. 55-61
    • Weyman, P.D.1    Pratte, B.2    Thiel, T.3
  • 183
    • 60849087991 scopus 로고    scopus 로고
    • Quantitative overview of N2 fixation in Nostoc punctiforme ATCC 29133 through cellular enrichments and iTRAQ shotgun proteomics
    • Ow SY, J Noirel, T Cardona, et al. Quantitative overview of N2 fixation in Nostoc punctiforme ATCC 29133 through cellular enrichments and iTRAQ shotgun proteomics. J Proteome Res 2009; 8: 187-98.
    • (2009) J Proteome Res , vol.8 , pp. 187-198
    • Ow, S.Y.1    Noirel, J.2    Cardona, T.3
  • 184
    • 0027495919 scopus 로고
    • Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis
    • Thiel T. Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis. J Bacteriol 1993; 175: 6276-86.
    • (1993) J Bacteriol , vol.175 , pp. 6276-6286
    • Thiel, T.1
  • 185
    • 0034732820 scopus 로고    scopus 로고
    • Vanadium nitrogenase
    • Rehder D. Vanadium nitrogenase. J Inorg Biochem 2000; 80: 133-6.
    • (2000) J Inorg Biochem , vol.80 , pp. 133-136
    • Rehder, D.1
  • 186
    • 0029049235 scopus 로고
    • A second nitrogenase in vegetative cells of a heterocyst-forming cyanobacterium
    • Thiel T, Lyons EM, Erker JC, Ernst A. A second nitrogenase in vegetative cells of a heterocyst-forming cyanobacterium. Proc Natl Acad Sci USA 1995; 92: 9358-62.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9358-9362
    • Thiel, T.1    Lyons, E.M.2    Erker, J.C.3    Ernst, A.4
  • 187
    • 0029945968 scopus 로고    scopus 로고
    • Photodissimilation of fructose to H2 and CO2 by a dinitrogen-fixing cyanobacterium, Anabaena variabilis
    • Reddy PM, Spiller H, Albrecht SL, Shanmugam KT. Photodissimilation of fructose to H2 and CO2 by a dinitrogen-fixing cyanobacterium, Anabaena variabilis. Appl Environ Microbiol 1996; 62: 1220-6.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1220-1226
    • Reddy, P.M.1    Spiller, H.2    Albrecht, S.L.3    Shanmugam, K.T.4
  • 188
    • 40749159953 scopus 로고    scopus 로고
    • Effect of growth conditions on the hydrogen production with cyanobacterium Anabaena sp
    • Chen P-C, Fan S-H, Chiang C-L, Lee C-M. Effect of growth conditions on the hydrogen production with cyanobacterium Anabaena sp. strain CH3. Int J Hydrogen Energy 2008; 33: 1460-4.
    • (2008) strain CH3. Int J Hydrogen Energy , vol.33 , pp. 1460-1464
    • Chen, P.-C.1    Fan, S.-H.2    Chiang, C.-L.3    Lee, C.-M.4
  • 189
    • 42049094614 scopus 로고    scopus 로고
    • Transcription of hupSL in Anabaena variabilis ATCC 29413 is regulated by NtcA and not by hydrogen
    • Weyman PD, Pratte B, Thiel T. Transcription of hupSL in Anabaena variabilis ATCC 29413 is regulated by NtcA and not by hydrogen. Appl Environ Microbiol 2008; 74: 2103-10.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 2103-2110
    • Weyman, P.D.1    Pratte, B.2    Thiel, T.3
  • 190
    • 74849137425 scopus 로고    scopus 로고
    • Screening for biohydrogen production by cyanobacteria isolated from the Baltic Sea and Finnish lakes
    • Allahverdiyeva Y, Leino H, Saari L, et al. Screening for biohydrogen production by cyanobacteria isolated from the Baltic Sea and Finnish lakes. Int J Hydrogen Energy 2010; 33: 1117-27.
    • (2010) Int J Hydrogen Energy , vol.33 , pp. 1117-1127
    • Allahverdiyeva, Y.1    Leino, H.2    Saari, L.3
  • 191
    • 0002648566 scopus 로고    scopus 로고
    • Hydrogen production by photosynthetic bacteria: culture media, yields, and efficiencies
    • In: Miyake J, Matsunaga T, San Pietro A, Eds. Biohydrogen II: an approach to environmentally acceptable technology. London: Pergamon
    • Rocha JS, Barbosa MJ, Wijfells RH. Hydrogen production by photosynthetic bacteria: culture media, yields, and efficiencies. In: Miyake J, Matsunaga T, San Pietro A, Eds. Biohydrogen II: an approach to environmentally acceptable technology. London: Pergamon 2001; pp. 3-32.
    • (2001) , pp. 3-32
    • Rocha, J.S.1    Barbosa, M.J.2    Wijfells, R.H.3
  • 192
    • 0000365836 scopus 로고
    • Screening photosynthetic bacteria for hydrogen production from organic acids
    • Mao XX, Miyake J, Kawamura S. Screening photosynthetic bacteria for hydrogen production from organic acids. J Ferment Technol 1986; 64: 245-9.
    • (1986) J Ferment Technol , vol.64 , pp. 245-249
    • Mao, X.X.1    Miyake, J.2    Kawamura, S.3
  • 193
    • 0002357923 scopus 로고    scopus 로고
    • Charaterization of photosynthetic bacterium Rhodospirillum rubrum RV for hydrogen production
    • Nagamine Y, Kawasugi Y, Miyake M, Asada Y, Miyake J. Charaterization of photosynthetic bacterium Rhodospirillum rubrum RV for hydrogen production. J Mar Biotechnol 1996; 4: 34-7.
    • (1996) J Mar Biotechnol , vol.4 , pp. 34-37
    • Nagamine, Y.1    Kawasugi, Y.2    Miyake, M.3    Asada, Y.4    Miyake, J.5
  • 194
    • 0031973733 scopus 로고    scopus 로고
    • Actual and potential rates of hydrogen photoproduction by continuous culture of the purple non-sulphur bacterium Rhodospirillum capsulatus
    • Tsygankov AA, Fedorov AS, Laurinavichene TV, Gogotov IN, Rao KK, Hall DO. Actual and potential rates of hydrogen photoproduction by continuous culture of the purple non-sulphur bacterium Rhodospirillum capsulatus. Appl Microbiol Biotechnol 1998; 49: 102-7.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 102-107
    • Tsygankov, A.A.1    Fedorov, A.S.2    Laurinavichene, T.V.3    Gogotov, I.N.4    Rao, K.K.5    Hall, D.O.6
  • 195
    • 55049102575 scopus 로고    scopus 로고
    • Hydrogen production during stationary phase in purple photosynthetic bacteria
    • Melnicki MR, Bianchi L, De Philippis R, Melis A. Hydrogen production during stationary phase in purple photosynthetic bacteria. Int J Hydrogen Energy 2008; 33: 6525-34.
    • (2008) Int J Hydrogen Energy , vol.33 , pp. 6525-6534
    • Melnicki, M.R.1    Bianchi, L.2    De Philippis, R.3    Melis, A.4
  • 196
    • 39049092251 scopus 로고    scopus 로고
    • Characteristics of a new photosynthetic bacterial strain for hydrogen production and its application in wastewater treatment
    • Tao Y, He Y, Wu Y, et al. Characteristics of a new photosynthetic bacterial strain for hydrogen production and its application in wastewater treatment. Int J Hydrogen Energy 2008; 33: 963-73.
    • (2008) Int J Hydrogen Energy , vol.33 , pp. 963-973
    • Tao, Y.1    He, Y.2    Wu, Y.3
  • 198
    • 0036210881 scopus 로고    scopus 로고
    • Enhancement of hydrogen production by a photosynthetic bacterium mutant with reduced pigment
    • Kondo T, Arakawa M, Hirai T, Wakayama T, Hara M, Miyaye J. Enhancement of hydrogen production by a photosynthetic bacterium mutant with reduced pigment. J Biosci Bioeng 2002; 93: 145-50.
    • (2002) J Biosci Bioeng , vol.93 , pp. 145-150
    • Kondo, T.1    Arakawa, M.2    Hirai, T.3    Wakayama, T.4    Hara, M.5    Miyaye, J.6
  • 199
    • 19944413663 scopus 로고    scopus 로고
    • Metabolically engineered Rhodobacter sphaeroides RV strains for improved biohydrogen photoproduction combined with disposal of food wastes
    • Franchi E, Tosi C, Scolla G, Della Penna G, Rodriguez F, Pedroni PM. Metabolically engineered Rhodobacter sphaeroides RV strains for improved biohydrogen photoproduction combined with disposal of food wastes. Mar Biotechnol 2004; 6: 552-65.
    • (2004) Mar Biotechnol , vol.6 , pp. 552-565
    • Franchi, E.1    Tosi, C.2    Scolla, G.3    Della Penna, G.4    Rodriguez, F.5    Pedroni, P.M.6
  • 200
    • 70449083049 scopus 로고    scopus 로고
    • Increased biological hydrogen production by deletion of hydrogen-uptake system in photosynthetic bacteria
    • Liang Y, Wu X, Gan L, Xu H, Hu Z, Long M. Increased biological hydrogen production by deletion of hydrogen-uptake system in photosynthetic bacteria. Microbiol Res 2009; 164: 674-9.
    • (2009) Microbiol Res , vol.164 , pp. 674-679
    • Liang, Y.1    Wu, X.2    Gan, L.3    Xu, H.4    Hu, Z.5    Long, M.6
  • 201
    • 33947219284 scopus 로고    scopus 로고
    • Redirection of metabolism for biological hydrogen production
    • Rey FE, Heiniger EK, Harwood CS. Redirection of metabolism for biological hydrogen production. Appl Environ Microbiol 2007; 73: 1665-71.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1665-1671
    • Rey, F.E.1    Heiniger, E.K.2    Harwood, C.S.3
  • 203
    • 0003145131 scopus 로고
    • Wavelength dependence of photoproduction of hydrogen by Rhodopseudomonas rutila
    • Nogi Y, Akiba T, Horikoshi K. Wavelength dependence of photoproduction of hydrogen by Rhodopseudomonas rutila. Agric Biol Chem 1985; 49: 35-8.
    • (1985) Agric Biol Chem , vol.49 , pp. 35-38
    • Nogi, Y.1    Akiba, T.2    Horikoshi, K.3


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