메뉴 건너뛰기




Volumn 74, Issue 4, 2010, Pages 529-551

Nitrogen fixation and hydrogen metabolism in cyanobacteria

Author keywords

[No Author keywords available]

Indexed keywords

BIDIRECTIONAL HYDROGENASE; HYDROGEN; HYDROGENASE; MOLYBDENUM NITOGENASE; NITROGEN; NITROGENASE; UNCLASSIFIED DRUG; UPTAKE HYDROGENASE;

EID: 78650162210     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00033-10     Document Type: Review
Times cited : (327)

References (242)
  • 1
    • 38249032579 scopus 로고
    • Hydrogen metabolism of the unicellular cyanobacterium Chroococcidiopsis thermalis ATCC 29380
    • Almon, H., and P. Böger. 1988. Hydrogen metabolism of the unicellular cyanobacterium Chroococcidiopsis thermalis ATCC 29380. FEMS Microbiol. Lett. 49:445-449.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 445-449
    • Almon, H.1    Böger, P.2
  • 2
    • 78650129006 scopus 로고
    • Nickel-dependent uptake-hydrogenase activity in the blue-green alga Anabaena variabilis
    • Almon, H., and P. Böger. 1984. Nickel-dependent uptake-hydrogenase activity in the blue-green alga Anabaena variabilis. Z. Naturforsch. 39:90-94.
    • (1984) Z. Naturforsch. , vol.39 , pp. 90-94
    • Almon, H.1    Böger, P.2
  • 3
    • 54449090208 scopus 로고    scopus 로고
    • Optimization of metabolic capacity and flux through environmental cues to maximize hydrogen production by the cyanobacterium Arthospira (Spirulina) maxima
    • Ananyev, G., D. Carrieri, and C. G. Dismukes. 2008. Optimization of metabolic capacity and flux through environmental cues to maximize hydrogen production by the cyanobacterium Arthospira (Spirulina) maxima. Appl. Environ. Microbiol. 74:6102-6113.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 6102-6113
    • Ananyev, G.1    Carrieri, D.2    Dismukes, C.G.3
  • 4
    • 12344288213 scopus 로고    scopus 로고
    • 2by sulphur-deprived cells of the unicellular cyanobacteria Gloeocapsa alpicola and Synechocystis sp. PCC 6803 during dark incubation with methane or at various extracellular pH
    • 2 by sulphur-deprived cells of the unicellular cyanobacteria Gloeocapsa alpicola and Synechocystis sp. PCC 6803 during dark incubation with methane or at various extracellular pH. J. Appl. Microbiol. 98:114-120.
    • (2005) J. Appl. Microbiol. , vol.98 , pp. 114-120
    • Antal, T.K.1    Lindblad, P.2
  • 5
    • 33746909795 scopus 로고    scopus 로고
    • The bidirectional hydrogenase in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Antal, T. K., P. Oliveira, and P. Lindblad. 2006. The bidirectional hydrogenase in the cyanobacterium Synechocystis sp. strain PCC 6803. Int. J. Hydrogen Energy 31:114-120.
    • (2006) Int. J. Hydrogen Energy , vol.31 , pp. 114-120
    • Antal, T.K.1    Oliveira, P.2    Lindblad, P.3
  • 6
    • 0034082075 scopus 로고    scopus 로고
    • The bidirectional hydrogenase of Synechocystis PCC 6803 works as an electron valve during photosynthesis
    • Appel, J., S. Phunpruch, K. Steinmüller, and R. Schulz. 2000. The bidirectional hydrogenase of Synechocystis PCC 6803 works as an electron valve during photosynthesis. Arch. Microbiol. 173:333-338.
    • (2000) Arch. Microbiol. , vol.173 , pp. 333-338
    • Appel, J.1    Phunpruch, S.2    Steinmüller, K.3    Schulz, R.4
  • 7
    • 0032216314 scopus 로고    scopus 로고
    • Hydrogen metabolism in organisms with oxygenic photosynthesis: Hydrogenase as important regulatory devices for a proper redox poising?
    • Appel, J., and R. Schulz. 1998. Hydrogen metabolism in organisms with oxygenic photosynthesis: hydrogenase as important regulatory devices for a proper redox poising? J. Photochem. Photobiol. Biol. 47:1-11.
    • (1998) J. Photochem. Photobiol. Biol. , vol.47 , pp. 1-11
    • Appel, J.1    Schulz, R.2
  • 8
    • 0033967946 scopus 로고    scopus 로고
    • Heterologous expression of clostridial hydrogenase in the cyanobacterium Synechococcus PCC7942
    • Asada, Y., Y. Koike, J. Schnackenberg, M. Miyake, I. Uemura, and J. Miyake. 2000. Heterologous expression of clostridial hydrogenase in the cyanobacterium Synechococcus PCC7942. Biochim. Biophys. Acta 1490:269-278.
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 269-278
    • Asada, Y.1    Koike, Y.2    Schnackenberg, J.3    Miyake, M.4    Uemura, I.5    Miyake, J.6
  • 9
    • 33845522034 scopus 로고    scopus 로고
    • Identification of the glycosyl transferase required for synthesis of the the principal glycolipid characteristic of heterocysts of Anabaena sp strain PCC 7120
    • Awai, K., and C. Wolk. 2007. Identification of the glycosyl transferase required for synthesis of the the principal glycolipid characteristic of heterocysts of Anabaena sp strain PCC 7120. FEMS Microbiol. Lett. 266:98-102.
    • (2007) FEMS Microbiol. Lett. , vol.266 , pp. 98-102
    • Awai, K.1    Wolk, C.2
  • 10
    • 0036135161 scopus 로고    scopus 로고
    • Transcriptional regulation of Nostoc hydrogenases:effects of oxygen, hydrogen and nickel
    • Axelsson, R., and P. Lindblad. 2002. Transcriptional regulation of Nostoc hydrogenases:effects of oxygen, hydrogen and nickel. Appl. Environ. Microbiol. 68:444-447.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 444-447
    • Axelsson, R.1    Lindblad, P.2
  • 11
    • 34547747897 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes: Multiplicity in function and subunit composition
    • Battchikova, N., and E. M. Aro. 2007. Cyanobacterial NDH-1 complexes: multiplicity in function and subunit composition. Physiol. Plant. 13:22-32.
    • (2007) Physiol. Plant. , vol.13 , pp. 22-32
    • Battchikova, N.1    Aro, E.M.2
  • 12
    • 0027368519 scopus 로고
    • Growth of the cyanobacterium Anabaena on molecular nitrogen: NifJ is required when iron is limited
    • Bauer, C. C., L. Scappino, and R. Haselkorn. 1993. Growth of the cyanobacterium Anabaena on molecular nitrogen: NifJ is required when iron is limited. Proc. Natl. Acad. Sci. U. S. A. 90:8812-8816.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8812-8816
    • Bauer, C.C.1    Scappino, L.2    Haselkorn, R.3
  • 13
    • 0017843654 scopus 로고
    • Hydrogen metabolism in the facultative anoxygenic cyanobacteria (blue-green algae) Oscillatoria limnetica and Aphanothece halophytica
    • Belkin, S., and E. Padan. 1978. Hydrogen metabolism in the facultative anoxygenic cyanobacteria (blue-green algae) Oscillatoria limnetica and Aphanothece halophytica. Arch. Microbiol. 116:109-111.
    • (1978) Arch. Microbiol. , vol.116 , pp. 109-111
    • Belkin, S.1    Padan, E.2
  • 15
    • 0037388041 scopus 로고    scopus 로고
    • Nitrogen fixation nad photosynthetic oxygen evolution in cyanobacteria
    • Berman-Frank, I., P. Lundgren, and P. Falkowski. 2003. Nitrogen fixation nad photosynthetic oxygen evolution in cyanobacteria. Res. Microbiol. 154:157-164.
    • (2003) Res. Microbiol. , vol.154 , pp. 157-164
    • Berman-Frank, I.1    Lundgren, P.2    Falkowski, P.3
  • 16
    • 61349090418 scopus 로고    scopus 로고
    • Towards efficient hydrogen production: The impact of antenna size and external factors on electron transport dynamics in Synechocystis PCC 6803
    • Bernat, G., N. Waschewski, and M. Rögner. 2009. Towards efficient hydrogen production: the impact of antenna size and external factors on electron transport dynamics in Synechocystis PCC 6803. Photosynthesis Res. 99:205-216.
    • (2009) Photosynthesis Res. , vol.99 , pp. 205-216
    • Bernat, G.1    Waschewski, N.2    Rögner, M.3
  • 17
    • 44949091610 scopus 로고    scopus 로고
    • Characterization of diazotrophs containing Mo-independent nitrogenases, isolated from diverse natural environments
    • Betancourt, D. A., T. M. Loveless, J. Brown, and P. E. Bishop. 2008. Characterization of diazotrophs containing Mo-independent nitrogenases, isolated from diverse natural environments. Appl. Environ. Microbiol. 74:3471-3480.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 3471-3480
    • Betancourt, D.A.1    Loveless, T.M.2    Brown, J.3    Bishop, P.E.4
  • 18
    • 0000421181 scopus 로고
    • Genetics and molecular biology of alternative nitrogen fixing systems
    • Bishop, P., and R. D. Joerger. 1990. Genetics and molecular biology of alternative nitrogen fixing systems. Annu. Rev. Plant Physiol. Plant Mol. Biol. 41:109-125.
    • (1990) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.41 , pp. 109-125
    • Bishop, P.1    Joerger, R.D.2
  • 19
    • 0002369684 scopus 로고
    • Alternative nitrogen fixing systems
    • G. Stacey, R. H. Burris, and H. J. Evans (ed.), Chapman and Hill, New York, NY
    • Bishop, P., and R. Premakur. 1992. Alternative nitrogen fixing systems, p. 736-762. In G. Stacey, R. H. Burris, and H. J. Evans (ed.), Biological nitrogen fixation. Chapman and Hill, New York, NY.
    • (1992) Biological Nitrogen Fixation , pp. 736-762
    • Bishop, P.1    Premakur, R.2
  • 21
    • 0343265713 scopus 로고    scopus 로고
    • Regulation of nitrogen fixation in heterocyst-forming cyanobacteria
    • DOI 10.1016/S1360-1385(98)01290-4, PII S1360138598012904
    • Böhme, H. 1998. Regulation of nitrogen fixation in heterocyst-forming cyanobacteria. Trends Plant Sci. 3:346-351. (Pubitemid 28422238)
    • (1998) Trends in Plant Science , vol.3 , Issue.9 , pp. 346-351
    • Bohme, H.1
  • 22
    • 78650096881 scopus 로고    scopus 로고
    • Evidence against a common use of the diaphorase subunits by the bidirectional hydrogenase and by respiratory complex I in cyanobacteria
    • Boison, G., H. Bothe, A. Hansel, and P. Lindblad. 1998. Evidence against a common use of the diaphorase subunits by the bidirectional hydrogenase and by respiratory complex I in cyanobacteria. FEMS Microbiol. Lett. 37:281-288.
    • (1998) FEMS Microbiol. Lett. , vol.37 , pp. 281-288
    • Boison, G.1    Bothe, H.2    Hansel, A.3    Lindblad, P.4
  • 23
    • 0034028570 scopus 로고    scopus 로고
    • Transcriptional analysis of hydrogenase genes in the cyanobacteria Anacystis nidulans and Anabaena variabilis monitored by RT-PCR
    • Boison, G., H. Bothe, and O. Schmitz. 2000. Transcriptional analysis of hydrogenase genes in the cyanobacteria Anacystis nidulans and Anabaena variabilis monitored by RT-PCR. Curr. Microbiol. 40:315-321.
    • (2000) Curr. Microbiol. , vol.40 , pp. 315-321
    • Boison, G.1    Bothe, H.2    Schmitz, O.3
  • 25
    • 0031919675 scopus 로고    scopus 로고
    • Unusual gene arrangement of the bidirectional hydrogenase and functional analysis of its diaphorase subunit HoxU in respiration of the unicellular cyanobacterium Anacystis nidulans
    • DOI 10.1007/s002849900305
    • Boison, G., O. Schmitz, B. Schmitz, and H. Bothe. 1998. Unusual gene arrangement of the bidirectional hydrogenase and functional analysis of its diaphorase subunit HoxU in respiration of the unicellular cyanobacterium Anacystis nidulans. Curr. Microbiol. 36:253-258. (Pubitemid 28182904)
    • (1998) Current Microbiology , vol.36 , Issue.5 , pp. 253-258
    • Boison, G.1    Schmitz, O.2    Schmitz, B.3    Bothe, H.4
  • 26
    • 33750735729 scopus 로고    scopus 로고
    • The rice field cyanobacteria Anabaena azotica and Anabaena sp.CH1 express vanadium-dependent nitrogenase
    • Boison, G., C. Steingen, L. J. Stal, and H. Bothe. 2006. The rice field cyanobacteria Anabaena azotica and Anabaena sp.CH1 express vanadium-dependent nitrogenase. Archiv. Microbiol. 186:367-376.
    • (2006) Archiv. Microbiol. , vol.186 , pp. 367-376
    • Boison, G.1    Steingen, C.2    Stal, L.J.3    Bothe, H.4
  • 27
    • 0034609594 scopus 로고    scopus 로고
    • Hydrogen production by Anabaena variabilis PK84 under simulated outdoor conditions
    • Borodin, V. B., A. Tsygankov, K. K. Rao, and D. O. Hall. 2000. Hydrogen production by Anabaena variabilis PK84 under simulated outdoor conditions. Biotechnol. Bioeng. 69:479-485.
    • (2000) Biotechnol. Bioeng. , vol.69 , pp. 479-485
    • Borodin, V.B.1    Tsygankov, A.2    Rao, K.K.3    Hall, D.O.4
  • 28
    • 0014622103 scopus 로고
    • Ferredoxin als Kofaktor der cylischen Photophosphorylierung in einem zellfreien System aus der Blaualge Anacystis nidulans
    • Bothe, H. 1969. Ferredoxin als Kofaktor der cylischen Photophosphorylierung in einem zellfreien System aus der Blaualge Anacystis nidulans. Z. Naturforsch. 24b:1574-1582.
    • (1969) Z. Naturforsch. , vol.24 B , pp. 1574-1582
    • Bothe, H.1
  • 29
    • 0017850666 scopus 로고
    • Hydrogen metabolism in blue-green algae
    • Bothe, H., E. Distler, and G. Eisbrenner. 1978. Hydrogen metabolism in blue-green algae. Biochimie 60:277-289.
    • (1978) Biochimie , vol.60 , pp. 277-289
    • Bothe, H.1    Distler, E.2    Eisbrenner, G.3
  • 30
    • 0344180652 scopus 로고
    • Effect of 7-azatryptophan on nitrogen fixation and heterocyst formation in the blue-green alga Anabaena cylindrica
    • Bothe, H., and G. Eisbrenner. 1977. Effect of 7-azatryptophan on nitrogen fixation and heterocyst formation in the blue-green alga Anabaena cylindrica. Biochem. Physiol. Pflanz. 133:323-332.
    • (1977) Biochem. Physiol. Pflanz. , vol.133 , pp. 323-332
    • Bothe, H.1    Eisbrenner, G.2
  • 31
    • 84908705984 scopus 로고
    • The hydrogenase-nitrogenase relationship in nitrogen-fixing organisms
    • H. Bothe and A. Trebst (ed.), Springer, Berlin, Germany
    • Bothe, H., and G. Eisbrenner. 1981. The hydrogenase-nitrogenase relationship in nitrogen-fixing organisms, p. 141-150. In H. Bothe and A. Trebst (ed.), Biology of inorganic nitrogen and sulfur. Springer, Berlin, Germany.
    • (1981) Biology of Inorganic Nitrogen and Sulfur , pp. 141-150
    • Bothe, H.1    Eisbrenner, G.2
  • 32
    • 78650130275 scopus 로고
    • Some properties of phytoflavin isolated from the blue-green alga Anacystis nidulans
    • H. Kamin (ed.), University Park Press-Butterworth, Baltimore, MD
    • Bothe, H., P. Hemmerich, and H. Sund. 1971. Some properties of phytoflavin isolated from the blue-green alga Anacystis nidulans, p. 211-237. In H. Kamin (ed.), Flavins and flavoproteins. University Park Press-Butterworth, Baltimore, MD.
    • (1971) Flavins and Flavoproteins , pp. 211-237
    • Bothe, H.1    Hemmerich, P.2    Sund, H.3
  • 33
    • 0000727357 scopus 로고
    • Electron donation to nitrogenase in heterocysts
    • Bothe, H., and G. Neuer. 1988. Electron donation to nitrogenase in heterocysts. Methods Enzymol. 167:496-501.
    • (1988) Methods Enzymol , vol.167 , pp. 496-501
    • Bothe, H.1    Neuer, G.2
  • 34
    • 49649101332 scopus 로고    scopus 로고
    • Maximizing hydrogen production by cyanobacteria
    • Bothe, H., S. Winkelmann, and G. Boison. 2008. Maximizing hydrogen production by cyanobacteria. Z. Naturforsch. 63c:226-232.
    • (2008) Z. Naturforsch. , vol.63 C , pp. 226-232
    • Bothe, H.1    Winkelmann, S.2    Boison, G.3
  • 36
    • 43549097823 scopus 로고    scopus 로고
    • Host-dependent expression of Rhizobium leguminosarum bv viciae hydrogenase is controlled at the transcriptional and posttranslational levels in legume nodules
    • Brito, B., A. Toffanin, R. I. Prieto, J. Imperial, T. Ruiz-Arguesco, and R. M. Palacios. 2008. Host-dependent expression of Rhizobium leguminosarum bv viciae hydrogenase is controlled at the transcriptional and posttranslational levels in legume nodules. Mol. Plant Microbe Interact. 21:597-604.
    • (2008) Mol. Plant Microbe Interact. , vol.21 , pp. 597-604
    • Brito, B.1    Toffanin, A.2    Prieto, R.I.3    Imperial, J.4    Ruiz-Arguesco, T.5    Palacios, R.M.6
  • 37
    • 0024720297 scopus 로고
    • Excision of an 11-kilobase-pair DNA element from within the nifD gene in Anabaena variabilis heteterocysts
    • Brusca, J. S., C. D. Carrasco, and J. W. Golden. 1989. Excision of an 11-kilobase-pair DNA element from within the nifD gene in Anabaena variabilis heteterocysts. J. Bacteriol. 171:4138-4145.
    • (1989) J. Bacteriol. , vol.171 , pp. 4138-4145
    • Brusca, J.S.1    Carrasco, C.D.2    Golden, J.W.3
  • 38
    • 0035956906 scopus 로고    scopus 로고
    • Expression of the Anabaena hetR gene from a copper-regulated promoter leads to heterocyst differentiation under repressing conditions
    • Buikema, W. J., and R. Haselkorn. 2001. Expression of the Anabaena hetR gene from a copper-regulated promoter leads to heterocyst differentiation under repressing conditions. Proc. Natl. Acad. Sci. U. S. A. 98:2729-2734.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2729-2734
    • Buikema, W.J.1    Haselkorn, R.2
  • 39
    • 0016727167 scopus 로고
    • Nitrogen fixation in bacteria and higher plants
    • Burns, R. C., and R. W. F. Hardy. 1975. Nitrogen fixation in bacteria and higher plants. Mol. Biol. Biochem. Biophys. 21:1-189.
    • (1975) Mol. Biol. Biochem. Biophys. , vol.21 , pp. 1-189
    • Burns, R.C.1    Hardy, R.W.F.2
  • 40
    • 55049127127 scopus 로고    scopus 로고
    • Optimization of media nutrient composition for increased photofermentative hydrogen production by Synechocystis sp PCC 6803
    • Burrows, E. H., F. W. R. Chaplen, and R. L. Ely. 2008. Optimization of media nutrient composition for increased photofermentative hydrogen production by Synechocystis sp PCC 6803. Int. J. Hydrogen Energy 33:6092-6099.
    • (2008) Int. J. Hydrogen Energy , vol.33 , pp. 6092-6099
    • Burrows, E.H.1    Chaplen, F.W.R.2    Ely, R.L.3
  • 41
    • 69149092509 scopus 로고    scopus 로고
    • Optimization of pH and nitrogen for enhanced hydrogen production by Synechocystis sp PCC 6803 via statistical and machine learning methods
    • Burrows, E. H., W. K. Wong, X. Fern, F. W. R. Chaplen, and R. L. Ely. 2009. Optimization of pH and nitrogen for enhanced hydrogen production by Synechocystis sp PCC 6803 via statistical and machine learning methods. Biotechnol. Prog. 25:1009-1017.
    • (2009) Biotechnol. Prog. , vol.25 , pp. 1009-1017
    • Burrows, E.H.1    Wong, W.K.2    Fern, X.3    Chaplen, F.W.R.4    Ely, R.L.5
  • 42
    • 0034995651 scopus 로고    scopus 로고
    • The role of HetN in maintenance of the heterocyst pattern in Anabaena sp PCC 7120
    • Callahan, S. M., and W. J. Buikema. 2001. The role of HetN in maintenance of the heterocyst pattern in Anabaena sp PCC 7120. Mol. Microbiol. 40:941-950.
    • (2001) Mol. Microbiol. , vol.40 , pp. 941-950
    • Callahan, S.M.1    Buikema, W.J.2
  • 43
    • 24344433943 scopus 로고    scopus 로고
    • Heterocyst-specific excision of the Anabaena strain PCC 7120 hupL element requires xisC
    • Carrasco, C. D., S. D. Holliday, A. Hansel, P. Lindblad, and J. W. Golden. 2005. Heterocyst-specific excision of the Anabaena strain PCC 7120 hupL element requires xisC. J. Bacteriol. 187:6031-6038.
    • (2005) J. Bacteriol. , vol.187 , pp. 6031-6038
    • Carrasco, C.D.1    Holliday, S.D.2    Hansel, A.3    Lindblad, P.4    Golden, J.W.5
  • 44
    • 0028948169 scopus 로고
    • Evidence for the occurrence of an alternative nitrogenase system in Azospirillum brasilense
    • Chakraborty, B., and K. R. Samaddar. 1995. Evidence for the occurrence of an alternative nitrogenase system in Azospirillum brasilense. FEMS Microbiol. Lett. 127:127-131.
    • (1995) FEMS Microbiol. Lett. , vol.127 , pp. 127-131
    • Chakraborty, B.1    Samaddar, K.R.2
  • 45
    • 0029862734 scopus 로고    scopus 로고
    • Purification and characterization of the vnf-encoded aponitrogenase from Azotobacter vinelandii
    • Chatterjee, R., R. M. Allen, P. W. Ludden, and V. K. Shah. 1996. Purification and characterization of the vnf-encoded aponitrogenase from Azotobacter vinelandii. J. Biol. Chem. 271:6819-6826.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6819-6826
    • Chatterjee, R.1    Allen, R.M.2    Ludden, P.W.3    Shah, V.K.4
  • 46
    • 0031021946 scopus 로고    scopus 로고
    • Characterization of VNFG, the delta subunit of the vnf-encoded apodinitrogenase from Azotobacter vinelandii: Implications for its role in the formation of functional dinitrogenase 2
    • Chatterjee, R., P. W. Ludden, and U. K. Shah. 1997. Characterization of VNFG, the delta subunit of the vnf-encoded apodinitrogenase from Azotobacter vinelandii: implications for its role in the formation of functional dinitrogenase 2. J. Biol. Chem. 272:3758-3765.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3758-3765
    • Chatterjee, R.1    Ludden, P.W.2    Shah, U.K.3
  • 47
    • 0034128057 scopus 로고    scopus 로고
    • Analysis of genes encoding an alternative nitrogenase in the archaeon Methanosarcina barkeri 227
    • Chien, Y.-T., V. Auerbruch, A. D. Brabban, and S. H. Zinder. 2000. Analysis of genes encoding an alternative nitrogenase in the archaeon Methanosarcina barkeri 227. J. Bacteriol. 182:3247-3253.
    • (2000) J. Bacteriol. , vol.182 , pp. 3247-3253
    • Chien, Y.-T.1    Auerbruch, V.2    Brabban, A.D.3    Zinder, S.H.4
  • 48
    • 18144370093 scopus 로고    scopus 로고
    • Effects of a simulated martian UV flux on the cyanobacterium, Chroococcidiopsis sp. 029
    • Cockell, C. S., A. C. Schuerger, D. Billi, E. I. Friedmann, and C. Panitz. 2005. Effects of a simulated martian UV flux on the cyanobacterium, Chroococcidiopsis sp. 029. Astrobiology 5:127-140.
    • (2005) Astrobiology , vol.5 , pp. 127-140
    • Cockell, C.S.1    Schuerger, A.C.2    Billi, D.3    Friedmann, E.I.4    Panitz, C.5
  • 49
    • 0033978251 scopus 로고    scopus 로고
    • Succinate:quinole oxidoreductases in the cyanobacterium Synechocystis sp. PCC 6803: Presence and function in metabolism and electron transport
    • Cooley, C., C. A. Howitt, and W. F. J. Vermaas. 2000. Succinate:quinole oxidoreductases in the cyanobacterium Synechocystis sp. PCC 6803: presence and function in metabolism and electron transport. J. Bacteriol. 182:714722.
    • (2000) J. Bacteriol. , vol.182 , pp. 714722
    • Cooley, C.1    Howitt, C.A.2    Vermaas, W.F.J.3
  • 51
    • 1542286924 scopus 로고    scopus 로고
    • Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp. strain PCC 6803 deficient in the type I NADH-dehydrogenase complex
    • Cournac, L., G. Guedeney, G. Peltier, and P. M. Vignais. 2004. Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp. strain PCC 6803 deficient in the type I NADH-dehydrogenase complex. J. Bacteriol. 186:1737-1746.
    • (2004) J. Bacteriol. , vol.186 , pp. 1737-1746
    • Cournac, L.1    Guedeney, G.2    Peltier, G.3    Vignais, P.M.4
  • 52
    • 0037181128 scopus 로고    scopus 로고
    • Sucrose is involved in the diazotrophic metabolism of the heterocyst-forming cyanobacterium Anabaena sp
    • Currati, L., E. Flores, and G. Salerno. 2002. Sucrose is involved in the diazotrophic metabolism of the heterocyst-forming cyanobacterium Anabaena sp. FEBS Lett. 513:175-178.
    • (2002) FEBS Lett. , vol.513 , pp. 175-178
    • Currati, L.1    Flores, E.2    Salerno, G.3
  • 54
    • 65349159139 scopus 로고    scopus 로고
    • Diversity and transcription of proteases involved in the maturation of hydrogenases in Nostoc punctiforme ATCC 29133 and Nostoc sp strain PCC 7120
    • Devine, E., M. Holmquist, K. Stensjö, and P. Lindblad. 2009. Diversity and transcription of proteases involved in the maturation of hydrogenases in Nostoc punctiforme ATCC 29133 and Nostoc sp strain PCC 7120. BMC Microbiol. 9:1-19.
    • (2009) BMC Microbiol. , vol.9 , pp. 1-19
    • Devine, E.1    Holmquist, M.2    Stensjö, K.3    Lindblad, P.4
  • 55
    • 46849118817 scopus 로고    scopus 로고
    • Marine diazotrophic cyanobacteria: Out of the blue
    • Diez, B., B. Bergman, and R. El-Shehawy. 2009. Marine diazotrophic cyanobacteria: out of the blue. Plant Biotechnol. 25:221-225.
    • (2009) Plant Biotechnol. , vol.25 , pp. 221-225
    • Diez, B.1    Bergman, B.2    El-Shehawy, R.3
  • 56
    • 0023213956 scopus 로고
    • Ethane formation from acetylene as a potential test for vanadium nitrogenase in vivo
    • Dilworth, M. J., R. R. Eady, R. L. Robson, and R. W. Miller. 1987. Ethane formation from acetylene as a potential test for vanadium nitrogenase in vivo. Nature 327:167-168.
    • (1987) Nature , vol.327 , pp. 167-168
    • Dilworth, M.J.1    Eady, R.R.2    Robson, R.L.3    Miller, R.W.4
  • 57
    • 0025737692 scopus 로고
    • Hydrazine is a byproduct of dinitrogen reduction by the vanadium-nitrogenase from Azotobacter chroococcum
    • Dilworth, M. J., and R. R. Eady. 1991. Hydrazine is a byproduct of dinitrogen reduction by the vanadium-nitrogenase from Azotobacter chroococcum. Biochem. J. 277:465-468.
    • (1991) Biochem. J. , vol.277 , pp. 465-468
    • Dilworth, M.J.1    Eady, R.R.2
  • 58
    • 0015271866 scopus 로고
    • Hydrogenase in legume root nodule bacteroids, occurrence and properties
    • Dixon, R. O. D. 1972. Hydrogenase in legume root nodule bacteroids, occurrence and properties. Arch. Microbiol. 85:193-201.
    • (1972) Arch. Microbiol. , vol.85 , pp. 193-201
    • Dixon, R.O.D.1
  • 59
    • 0001219252 scopus 로고    scopus 로고
    • Structure-function relationship of alternative nitrogenase
    • Eady, R. R. 1996. Structure-function relationship of alternative nitrogenase. Chem. Rev. 96:3013-3030.
    • (1996) Chem. Rev. , vol.96 , pp. 3013-3030
    • Eady, R.R.1
  • 60
    • 33847171444 scopus 로고    scopus 로고
    • Prokaryotic life in a potash-polluted marsh with emphasis on N-metabolizing microorganisms
    • Eilmus, S., C. Rösch, and H. Bothe. 2007. Prokaryotic life in a potash-polluted marsh with emphasis on N-metabolizing microorganisms. Environ. Pollut. 146:478-491.
    • (2007) Environ. Pollut. , vol.146 , pp. 478-491
    • Eilmus, S.1    Rösch, C.2    Bothe, H.3
  • 61
    • 0037031703 scopus 로고    scopus 로고
    • Nitrogenase MoFe-protein at 1.16 ångstrom resolution: A central ligand in the FeMo-cofactor
    • Einsle, O., F. A. Tezcan, A. Andrade, B. Schmid, M. Yoshida, J. B. Howard, and D. C. Rees. 2002. Nitrogenase MoFe-protein at 1.16 Ångstrom resolution: a central ligand in the FeMo-cofactor. Science 297:1696-1700.
    • (2002) Science , vol.297 , pp. 1696-1700
    • Einsle, O.1    Tezcan, F.A.2    Andrade, A.3    Schmid, B.4    Yoshida, M.5    Howard, J.B.6    Rees, D.C.7
  • 62
    • 33845427412 scopus 로고    scopus 로고
    • NrrA directly regulates expression of hetR during heterocyst differentiation in the cyanobacterium Anabaena sp. strain PCC 7120
    • Elhira, S., and M. Ohmori. 2006. NrrA directly regulates expression of hetR during heterocyst differentiation in the cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 188:8520-8525.
    • (2006) J. Bacteriol. , vol.188 , pp. 8520-8525
    • Elhira, S.1    Ohmori, M.2
  • 63
    • 0026291842 scopus 로고
    • Ocean anoxia and the concentration of molybdenum and vanadium in seawater
    • Emerson, S. R., and S. S. Huestedt. 1991. Ocean anoxia and the concentration of molybdenum and vanadium in seawater. Mar. Chem. 34:177-196.
    • (1991) Mar. Chem. , vol.34 , pp. 177-196
    • Emerson, S.R.1    Huestedt, S.S.2
  • 66
    • 0026684361 scopus 로고
    • Oxygen relations of nitrogen fixation in cyanobacteria
    • Fay, P. 1992. Oxygen relations of nitrogen fixation in cyanobacteria. Microbiol. Rev. 56:340-373.
    • (1992) Microbiol. Rev. , vol.56 , pp. 340-373
    • Fay, P.1
  • 67
    • 65449132371 scopus 로고    scopus 로고
    • Transcription profiles of hydrogenase related genes in the cyanobacterium Lyngbya majuscula CCAP 1446/4
    • Ferreira, D., F. A. L. Pinto, P. Morades-Ferreira, M. V. Mendez, and P. Tamagnini. 2009. Transcription profiles of hydrogenase related genes in the cyanobacterium Lyngbya majuscula CCAP 1446/4. BMC Microbiol. 9:67.
    • (2009) BMC Microbiol. , vol.9 , pp. 67
    • Ferreira, D.1    Pinto, F.A.L.2    Morades-Ferreira, P.3    Mendez, M.V.4    Tamagnini, P.5
  • 69
    • 0036398089 scopus 로고    scopus 로고
    • Chroococcidiopsis and heterocysts-differentiating cyanobacteria are each other's closest living relatives
    • Fewer, D., T. Friedl, and B. Büdel. 2002. Chroococcidiopsis and heterocysts-differentiating cyanobacteria are each other's closest living relatives. Mol. Phylogenet Evol. 23:82-90.
    • (2002) Mol. Phylogenet Evol. , vol.23 , pp. 82-90
    • Fewer, D.1    Friedl, T.2    Büdel, B.3
  • 70
    • 35348832336 scopus 로고    scopus 로고
    • Conformations generated during turnover of the Azotobacter vinelandii MoFe protein and their relationship to physiological function
    • Fisher, K., D. J. Lowe, P. Tavares, A. S. Pereira, B. H. Huynh, D. Edmondson, and W. E. Newton. 2007. Conformations generated during turnover of the Azotobacter vinelandii MoFe protein and their relationship to physiological function. J. Inorg. Biochem. 101:1649-1656.
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1649-1656
    • Fisher, K.1    Lowe, D.J.2    Tavares, P.3    Pereira, A.S.4    Huynh, B.H.5    Edmondson, D.6    Newton, W.E.7
  • 71
    • 0000415670 scopus 로고
    • Nitrogen fixation in Rhopalodia gibba, a diatom containing blue-greenish inclusions symbiotically
    • W. Schwemmler and H. E. A. Schenk (ed.), Walter de Gruyter & Co, Berlin, Germany
    • Floener, L., and H. Bothe. 1980. Nitrogen fixation in Rhopalodia gibba, a diatom containing blue-greenish inclusions symbiotically, p. 541-552. In W. Schwemmler and H. E. A. Schenk (ed.), Endocytobiology, endosymbiosis and cell biology. Walter de Gruyter & Co, Berlin, Germany.
    • (1980) Endocytobiology, Endosymbiosis and Cell Biology , pp. 541-552
    • Floener, L.1    Bothe, H.2
  • 72
    • 33748544291 scopus 로고    scopus 로고
    • Is the periplasm continuous in filamentous cyanobacteria?
    • Flores, E., A. Herrero, C. P. Wolk, and I. Maldener. 2006. Is the periplasm continuous in filamentous cyanobacteria? Trends Microbiol. 14:439-443.
    • (2006) Trends Microbiol. , vol.14 , pp. 439-443
    • Flores, E.1    Herrero, A.2    Wolk, C.P.3    Maldener, I.4
  • 73
    • 68949181269 scopus 로고    scopus 로고
    • Structure-function relationship of anaerobic gas-processing metalloenzymes
    • Fontecilla-Camps, J., P. Amara, C. Cavazzo, Y. Nicolet, and A. Volbeda. 2009. Structure-function relationship of anaerobic gas-processing metalloenzymes. Nature 460:814-822.
    • (2009) Nature , vol.460 , pp. 814-822
    • Fontecilla-Camps, J.1    Amara, P.2    Cavazzo, C.3    Nicolet, Y.4    Volbeda, A.5
  • 74
    • 33749416596 scopus 로고    scopus 로고
    • Characterization of diatom-cyanobacteria symbioses on the basis of nifH, hetR and 16S rRNA sequences
    • Foster, R., and J. Zehr. 2006. Characterization of diatom-cyanobacteria symbioses on the basis of nifH, hetR and 16S rRNA sequences. Environ. Mirobiol. 8:1913-1925.
    • (2006) Environ. Mirobiol. , vol.8 , pp. 1913-1925
    • Foster, R.1    Zehr, J.2
  • 75
    • 0027382485 scopus 로고
    • Molecular biology of hydrogen utilization in aerobic chemolithotrophs
    • Friedrich, B., and E. Schwartz. 1993. Molecular biology of hydrogen utilization in aerobic chemolithotrophs. Annu. Rev. Microbiol. 47:351-383.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 351-383
    • Friedrich, B.1    Schwartz, E.2
  • 76
    • 0036225678 scopus 로고    scopus 로고
    • The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity
    • Galagan, J. E., C. Nusbaum, A. Roy, et al. 2002. The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity. Genome 12:532-542.
    • (2002) Genome , vol.12 , pp. 532-542
    • Galagan, J.E.1    Nusbaum, C.2    Roy, A.3
  • 77
    • 42249086808 scopus 로고    scopus 로고
    • Microalgae and cyanobacteria: Food for thought
    • Gantar, M. S. 2008. Microalgae and cyanobacteria: food for thought. J. Phycol. 44:260-268.
    • (2008) J. Phycol. , vol.44 , pp. 260-268
    • Gantar, M.S.1
  • 78
    • 0017581329 scopus 로고
    • Occurrence of facultative anoxygenic photosythesis among filamentous and unicellular cyanobacteria
    • Garlick, S., A. Oren, and E. Padan. 1977. Occurrence of facultative anoxygenic photosythesis among filamentous and unicellular cyanobacteria. J. Bacteriol. 129:623-629.
    • (1977) J. Bacteriol. , vol.129 , pp. 623-629
    • Garlick, S.1    Oren, A.2    Padan, E.3
  • 80
    • 3242762039 scopus 로고
    • Zur Entwicklungsgeschichte der Epithemiaceae Epithemia, Rhopalodia und Denticula (Diatomophyceae) und ihre vermutlichen symbiontischen Späroidkörper
    • Geitler, L. 1977. Zur Entwicklungsgeschichte der Epithemiaceae Epithemia, Rhopalodia und Denticula (Diatomophyceae) und ihre vermutlichen symbiontischen Späroidkörper. Plant Syst. Evol. 128:265-275.
    • (1977) Plant Syst. Evol. , vol.128 , pp. 265-275
    • Geitler, L.1
  • 83
    • 0017871027 scopus 로고
    • Plasma membrane architecture of Anabaena cylindrica: Occurrence of microplasmodesmata and changes associated with heterocyst development and the cell cycle
    • Giddings, J. W., and L. A. Staehelin. 1978. Plasma membrane architecture of Anabaena cylindrica: occurrence of microplasmodesmata and changes associated with heterocyst development and the cell cycle. Eur. J. Cell Biol. 16:235-249.
    • (1978) Eur. J. Cell Biol. , vol.16 , pp. 235-249
    • Giddings, J.W.1    Staehelin, L.A.2
  • 84
    • 0347994995 scopus 로고    scopus 로고
    • Heterocyst development in Anabaena
    • Golden, J. W., and H. S. Yoon. 2003. Heterocyst development in Anabaena. Curr. Opin. Microbiol. 6:557-563.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 557-563
    • Golden, J.W.1    Yoon, H.S.2
  • 86
    • 0019384375 scopus 로고
    • Enzyme activities related to cyanophycin metabolism in heterocysts and vegetative cells of Anabaena spp
    • Gupta, M., and N. G. Carr. 1981. Enzyme activities related to cyanophycin metabolism in heterocysts and vegetative cells of Anabaena spp. J. Gen. Microbiol. 125:17-23.
    • (1981) J. Gen. Microbiol. , vol.125 , pp. 17-23
    • Gupta, M.1    Carr, N.G.2
  • 88
    • 33847137761 scopus 로고    scopus 로고
    • Inhibition of respiration and nitrate assimlation enhances photohydrogen evolution under low oxygen concentrations in Synechocystis sp PCC 6803
    • Gutthann, F., M. Egert, A. Marques, and J. Appel. 2007. Inhibition of respiration and nitrate assimlation enhances photohydrogen evolution under low oxygen concentrations in Synechocystis sp PCC 6803. Biochim. Biophys. Acta 1767:161-169.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 161-169
    • Gutthann, F.1    Egert, M.2    Marques, A.3    Appel, J.4
  • 89
    • 0033009408 scopus 로고    scopus 로고
    • Flavodoxin accumulation contributes to enhanced cyclic electron flow around photosystem I in salt stressed cells of Synechocystis sp strain PCC 6803
    • Hagemann, M., R. Jeanjean, S. Fulda, M. Havaux, F. Joset, and N. Erdmann. 1999. Flavodoxin accumulation contributes to enhanced cyclic electron flow around photosystem I in salt stressed cells of Synechocystis sp strain PCC 6803. Physiol. Plant. 105:670-678.
    • (1999) Physiol. Plant. , vol.105 , pp. 670-678
    • Hagemann, M.1    Jeanjean, R.2    Fulda, S.3    Havaux, M.4    Joset, F.5    Erdmann, N.6
  • 90
    • 0000148282 scopus 로고
    • The potential applications of cyanobacterial photosythesis for clean technologies
    • Hall, D. O., S. A. Markov, Y. Watanabe, and K. K. Rao. 1995. The potential applications of cyanobacterial photosythesis for clean technologies. Photosynth. Res. 46:159-167.
    • (1995) Photosynth. Res. , vol.46 , pp. 159-167
    • Hall, D.O.1    Markov, S.A.2    Watanabe, Y.3    Rao, K.K.4
  • 91
    • 0036618091 scopus 로고    scopus 로고
    • Hydrogenases in green algae. Do they save the algae's life and solve our energy problems?
    • Happe, T., A. Hemschemeier, M. Winkler, and A. Kaminski. 2002. Hydrogenases in green algae. Do they save the algae's life and solve our energy problems? Trends Plant Sci. 7:246-250.
    • (2002) Trends Plant Sci. , vol.7 , pp. 246-250
    • Happe, T.1    Hemschemeier, A.2    Winkler, M.3    Kaminski, A.4
  • 92
    • 0343986359 scopus 로고    scopus 로고
    • Transcriptional and mutational analysis of the uptake hydrogenase of the filamentous cyanobacterium Anabaena variabilis
    • Happe, T., K. Schütz, and H. Böhme. 2000. Transcriptional and mutational analysis of the uptake hydrogenase of the filamentous cyanobacterium Anabaena variabilis. J. Bacteriol. 182:1624-1631.
    • (2000) J. Bacteriol. , vol.182 , pp. 1624-1631
    • Happe, T.1    Schütz, K.2    Böhme, H.3
  • 93
    • 0027095688 scopus 로고
    • Developmentally regulated gene rearrangements in prokaryotes
    • Haselkorn, R. 1992. Developmentally regulated gene rearrangements in prokaryotes. Annu. Rev. Genet. 26:113-130.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 113-130
    • Haselkorn, R.1
  • 98
    • 63349099755 scopus 로고    scopus 로고
    • Characterization of the hupLS promoter activity in Nostoc punctiforme ATCC 29133
    • Holmqvist, M., K. Stensjö, P. Oliveira, P. Lindberg, and P. Lindblad. 2009. Characterization of the hupLS promoter activity in Nostoc punctiforme ATCC 29133. BMC Microbiol. 9:54.
    • (2009) BMC Microbiol. , vol.9 , pp. 54
    • Holmqvist, M.1    Stensjö, K.2    Oliveira, P.3    Lindberg, P.4    Lindblad, P.5
  • 99
    • 0000955682 scopus 로고
    • The physiology and biochemistry of hydrogen metabolism in cyanobacteria
    • Houchins, J. P. 1984. The physiology and biochemistry of hydrogen metabolism in cyanobacteria. Biochim. Biophys. Acta 768:227-255.
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 227-255
    • Houchins, J.P.1
  • 100
    • 0019436382 scopus 로고
    • Comparative characterization of two distinct hydrogenases from Anabaena sp. strain 7120
    • Houchins, J. P., and R. H. Burris. 1981. Comparative characterization of two distinct hydrogenases from Anabaena sp. strain 7120. J. Bacteriol. 146:215-221.
    • (1981) J. Bacteriol. , vol.146 , pp. 215-221
    • Houchins, J.P.1    Burris, R.H.2
  • 101
    • 0019509252 scopus 로고
    • Occurrence and localization of two distinct hydrogenases in the heterocystous cyanobacterium Anabaena sp. strain 7120
    • Houchins, J. P., and R. H. Burris. 1981. Occurrence and localization of two distinct hydrogenases in the heterocystous cyanobacterium Anabaena sp. strain 7120. J. Bacteriol. 146:209-214.
    • (1981) J. Bacteriol. , vol.146 , pp. 209-214
    • Houchins, J.P.1    Burris, R.H.2
  • 103
    • 33846469977 scopus 로고    scopus 로고
    • Light-driven hydrogen production by a hydrid complex of a [NiFe]-hydrogenase and the cyanobacterial photosystem I
    • Ihara, M., H. Nakamoto, T. Kamachi, I. Okura, and M. Maeda. 2006b. Light-driven hydrogen production by a hydrid complex of a [NiFe]-hydrogenase and the cyanobacterial photosystem I. Photochem. Photobiol. 82:1677-1685.
    • (2006) Photochem. Photobiol. , vol.82 , pp. 1677-1685
    • Ihara, M.1    Nakamoto, H.2    Kamachi, T.3    Okura, I.4    Maeda, M.5
  • 105
    • 55549101294 scopus 로고    scopus 로고
    • An AbrB-like transcriptional regulator, Sll0822, is essential for the activation of nitrogen-regulated genes in Synechocystis sp. PCC 6803
    • DOI 10.1104/pp.108.123505
    • Ishii, A., and Y. Hihara. 2008. An AbrB-like transcriptional regulator, SII0822, is essential for the activation of nitrogen-regulated genes in Synechocystis sp. PCC6803. Plant Physiol. 148:660-670. (Pubitemid 352847624)
    • (2008) Plant Physiology , vol.148 , Issue.1 , pp. 660-670
    • Ishii, A.1    Hihara, Y.2
  • 107
    • 0037379232 scopus 로고    scopus 로고
    • Heterocyst-specific expression of patB, a gene required for nitrogen fixation in Anabaena strain PCC 7120
    • Jones, K. M., W. J. Buikema, and R. Haselkorn. 2003. Heterocyst-specific expression of patB, a gene required for nitrogen fixation in Anabaena strain PCC 7120. J. Bacteriol. 185:2306-2314.
    • (2003) J. Bacteriol. , vol.185 , pp. 2306-2314
    • Jones, K.M.1    Buikema, W.J.2    Haselkorn, R.3
  • 108
    • 49249085251 scopus 로고    scopus 로고
    • Purification. crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum
    • Kellers, P., H. Ogata, and W. Lubitz. 2008. Purification. crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum. Acta Crystallogr. F 64:719-722.
    • (2008) Acta Crystallogr. F , vol.64 , pp. 719-722
    • Kellers, P.1    Ogata, H.2    Lubitz, W.3
  • 109
    • 0001280606 scopus 로고
    • Localization of the reversible hydrogenase in cyanobacteria
    • Kentemich, T., M. Bahnweg, F. Mayer, and H. Bothe. 1989. Localization of the reversible hydrogenase in cyanobacteria. Z. Naturforsch. 44c:384-391.
    • (1989) Z. Naturforsch. , vol.44 C , pp. 384-391
    • Kentemich, T.1    Bahnweg, M.2    Mayer, F.3    Bothe, H.4
  • 110
    • 0026321293 scopus 로고
    • The reversible hydrogenase in Anacystis nidulans is a component of the cytoplasmic membrane
    • Kentemich, T., M. Casper, and H. Bothe. 1991. The reversible hydrogenase in Anacystis nidulans is a component of the cytoplasmic membrane. Naturwisssenschaften 78:559-560.
    • (1991) Naturwisssenschaften , vol.78 , pp. 559-560
    • Kentemich, T.1    Casper, M.2    Bothe, H.3
  • 111
    • 0002836262 scopus 로고
    • Evidence for the occurrence of the alternative, vanadium-containing nitrogenase in the cyanobacterium Anabaena variabilis
    • Kentemich, T., G. Danneberg, B. Hundeshagen, and H. Bothe. 1988. Evidence for the occurrence of the alternative, vanadium-containing nitrogenase in the cyanobacterium Anabaena variabilis. FEMS Microbiol. Lett. 51:19-24.
    • (1988) FEMS Microbiol. Lett. , vol.51 , pp. 19-24
    • Kentemich, T.1    Danneberg, G.2    Hundeshagen, B.3    Bothe, H.4
  • 112
    • 0000450350 scopus 로고
    • The expression of a third nitrogenase in the cyanobacterium Anabaena variabilis
    • Kentemich, T., G. Haverkamp, and H. Bothe. 1991. The expression of a third nitrogenase in the cyanobacterium Anabaena variabilis. Z. Naturforsch. 46c:217-111.
    • (1991) Z. Naturforsch. , vol.46 C , pp. 217-1111
    • Kentemich, T.1    Haverkamp, G.2    Bothe, H.3
  • 113
    • 0031014709 scopus 로고    scopus 로고
    • Nitrogenase phylogeny and the molydenum dependence of nitrogen fixation in Methanococcus maripaludis
    • Kessler, P. S., J. McLarnan, and J. A. Leigh. 1997. Nitrogenase phylogeny and the molydenum dependence of nitrogen fixation in Methanococcus maripaludis. J. Bacteriol. 179:541-543.
    • (1997) J. Bacteriol. , vol.179 , pp. 541-543
    • Kessler, P.S.1    McLarnan, J.2    Leigh, J.A.3
  • 114
    • 27844439455 scopus 로고    scopus 로고
    • Nutritional and therapeutic potential of Spirulina
    • Khan, Z., P. Bhadouria, and P. Bisen. 2005. Nutritional and therapeutic potential of Spirulina. Curr. Pharm. Biotechnol. 6:373-379.
    • (2005) Curr. Pharm. Biotechnol. , vol.6 , pp. 373-379
    • Khan, Z.1    Bhadouria, P.2    Bisen, P.3
  • 115
    • 8644227726 scopus 로고    scopus 로고
    • Different functions of HetR, a master regulator of heterocyst differentiation in Anabaena sp. PCC 7120, can be separated by mutation
    • Khudyakov, I. Y., and J. W. Golden. 2004. Different functions of HetR, a master regulator of heterocyst differentiation in Anabaena sp. PCC 7120, can be separated by mutation. Proc. Natl. Acad. Sci. U. S. A. 101:16040-16045.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16040-16045
    • Khudyakov, I.Y.1    Golden, J.W.2
  • 116
    • 67349247430 scopus 로고    scopus 로고
    • Transcriptional regulation of the bidirectional hydrogenase in the cyanobacterium Synechocystis 6803
    • Kiss, E., P. B. Kos, and I. Vass. 2009. Transcriptional regulation of the bidirectional hydrogenase in the cyanobacterium Synechocystis 6803. J. Biotechnol. 142:31-37.
    • (2009) J. Biotechnol. , vol.142 , pp. 31-37
    • Kiss, E.1    Kos, P.B.2    Vass, I.3
  • 117
    • 63549101771 scopus 로고    scopus 로고
    • Latitudinal distribution of diazotrophs and their nitrogen fixation in the tropical and subtropical western North Pacific
    • Kitajima, S., F. Hashihama, and S. Takeda. 2009. Latitudinal distribution of diazotrophs and their nitrogen fixation in the tropical and subtropical western North Pacific. Limnol. Oceanogr. 54:537-547.
    • (2009) Limnol. Oceanogr. , vol.54 , pp. 537-547
    • Kitajima, S.1    Hashihama, F.2    Takeda, S.3
  • 118
    • 0032032876 scopus 로고    scopus 로고
    • Anaerobic reduction of ethene to ethane in an enrichment culture
    • Koene-Cottaar, F. H. M., and G. Schraa. 1998. Anaerobic reduction of ethene to ethane in an enrichment culture. FEMS Microbiol. Ecol. 25:251-256.
    • (1998) FEMS Microbiol. Ecol. , vol.25 , pp. 251-256
    • Koene-Cottaar, F.H.M.1    Schraa, G.2
  • 119
    • 1542309304 scopus 로고
    • Appearance of a reversible hydrogenase activity in Anabaena cylindrica grown in high light
    • Laczkó, I. 1986. Appearance of a reversible hydrogenase activity in Anabaena cylindrica grown in high light. Physiol. Plant 67:634-637.
    • (1986) Physiol. Plant , vol.67 , pp. 634-637
    • Laczkó, I.1
  • 120
    • 0015212999 scopus 로고
    • Pyruvate:ferredoxin oxidoreductase and its activation by ATP in the blue-green alga Anabaena variabilis
    • Leach, C. K., and N. G. Carr. 1971. Pyruvate:ferredoxin oxidoreductase and its activation by ATP in the blue-green alga Anabaena variabilis. Biochim. Biophys. Acta 245:165-174.
    • (1971) Biochim. Biophys. Acta , vol.245 , pp. 165-174
    • Leach, C.K.1    Carr, N.G.2
  • 122
    • 0345306164 scopus 로고    scopus 로고
    • An increase in the level of oxoglutarate promotes heterocyst development in the cyanobacterium Anabaena sp. strain 7120
    • Li, J. H., S. Laurent, V. Konde, S. Bedu, and C. C. Zhang. 2003. An increase in the level of oxoglutarate promotes heterocyst development in the cyanobacterium Anabaena sp. strain 7120. Microbiol. 149:3257-3263.
    • (2003) Microbiol. , vol.149 , pp. 3257-3263
    • Li, J.H.1    Laurent, S.2    Konde, V.3    Bedu, S.4    Zhang, C.C.5
  • 123
    • 1642489154 scopus 로고    scopus 로고
    • Expression of cyanobacterial genes involved in heterocyst differentiation and dinitrogen fixation along a plant symbiosis development profile
    • Liang, C.-M., M. Ekman, and B. Bergman. 2004. Expression of cyanobacterial genes involved in heterocyst differentiation and dinitrogen fixation along a plant symbiosis development profile. Mol. Plant Microbe Interact. 17:436-443.
    • (2004) Mol. Plant Microbe Interact. , vol.17 , pp. 436-443
    • Liang, C.-M.1    Ekman, M.2    Bergman, B.3
  • 124
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindal, M., and F. J. Florencio. 2003. Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc. Natl. Acad. Sci. U. S. A. 100:16107-16112.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 16107-16112
    • Lindal, M.1    Florencio, F.J.2
  • 126
    • 33747039506 scopus 로고    scopus 로고
    • 2by Anabaena variabilis mutant PK84 dense cultures exposed to nitrogen limitations
    • 2 by Anabaena variabilis mutant PK84 dense cultures exposed to nitrogen limitations. Int. J. Hydrogen Energy 31:1591-1596.
    • (2006) Int. J. Hydrogen Energy , vol.31 , pp. 1591-1596
    • Liu, J.G.1    Bukatin, V.E.2    Tsygankov, A.A.3
  • 127
    • 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., J. Liu, Z. Chen, B. Bleijlevens, W. Roseboom, and S. P. Albracht. 2007. 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. 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
  • 128
    • 35349025902 scopus 로고    scopus 로고
    • Cross-talk between iron and nitrogen regulatory networks in Anabaena (Nostoc) PCC 7120: Identification of the overlapping genes in FurA and Ntc regulons
    • Lopez-Gomollon, S., J. A. Hernandez, S. Pellicer, V. E. Angarica, M. L. Peleato, and M. F. Fillat. 2007. Cross-talk between iron and nitrogen regulatory networks in Anabaena (Nostoc) PCC 7120: identification of the overlapping genes in FurA and Ntc regulons. J. Mol. Biol. 374:267-281.
    • (2007) J. Mol. Biol. , vol.374 , pp. 267-281
    • Lopez-Gomollon, S.1    Hernandez, J.A.2    Pellicer, S.3    Angarica, V.E.4    Peleato, M.L.5    Fillat, M.F.6
  • 129
    • 0032821355 scopus 로고    scopus 로고
    • Identification of genes unique to Mo-independent nitrogenase systems in diverse diazotrophs
    • Loveless, T. M., and P. E. Bishop. 1999. Identification of genes unique to Mo-independent nitrogenase systems in diverse diazotrophs. Can. J. Microbiol. 45:312-317.
    • (1999) Can. J. Microbiol. , vol.45 , pp. 312-317
    • Loveless, T.M.1    Bishop, P.E.2
  • 130
    • 0032851747 scopus 로고    scopus 로고
    • Isolation of nitrogen-fixing bacteria containing molybdenum-independent nitrogenases from natural environments
    • Loveless, T. M., J. R. Saah, and P. E. Bishop. 1999. Isolation of nitrogen-fixing bacteria containing molybdenum-independent nitrogenases from natural environments. Appl. Environ. Microbiol. 65:4223-4225.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4223-4225
    • Loveless, T.M.1    Saah, J.R.2    Bishop, P.E.3
  • 131
    • 74949093472 scopus 로고    scopus 로고
    • Wiring photosystem I for direct solar hydrogen production
    • Lubner, C. E., R. A. Grimme, D. A. Bryant, and J. H. Golbeck. 2010. Wiring photosystem I for direct solar hydrogen production. Biochemistry 49:404-414.
    • (2010) Biochemistry , vol.49 , pp. 404-414
    • Lubner, C.E.1    Grimme, R.A.2    Bryant, D.A.3    Golbeck, J.H.4
  • 132
    • 33845369271 scopus 로고    scopus 로고
    • Occurrence of hydrogenases in cyanobacteria and anoxygenic photosynthetic bacteria: Implications for the phylogenetic origin of cyanobacterial and algal hydrogenases
    • Ludwig, M., R. Schulz-Friedrich, and J. Appel. 2006. Occurrence of hydrogenases in cyanobacteria and anoxygenic photosynthetic bacteria: implications for the phylogenetic origin of cyanobacterial and algal hydrogenases. J. Mol. Evol. 63:758-768.
    • (2006) J. Mol. Evol. , vol.63 , pp. 758-768
    • Ludwig, M.1    Schulz-Friedrich, R.2    Appel, J.3
  • 133
    • 0022508830 scopus 로고
    • Estimation of gene expression in heterocysts of Anabaena variabilis by using DNA-RNA hybridization
    • Lynn, M. E., J. A. Bantle, and J. D. Ownby. 1986. Estimation of gene expression in heterocysts of Anabaena variabilis by using DNA-RNA hybridization. J. Bacteriol. 167:940-946.
    • (1986) J. Bacteriol. , vol.167 , pp. 940-946
    • Lynn, M.E.1    Bantle, J.A.2    Ownby, J.D.3
  • 135
    • 34347385830 scopus 로고    scopus 로고
    • Inhibition of hydrogen uptake in Escherichia coli by expressing the hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803
    • Maeda, T., G. Vardar, W. T. Self, and T. K. Wood. 2007. Inhibition of hydrogen uptake in Escherichia coli by expressing the hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803. BMC Biotechnol. 7:25-37.
    • (2007) BMC Biotechnol. , vol.7 , pp. 25-37
    • Maeda, T.1    Vardar, G.2    Self, W.T.3    Wood, T.K.4
  • 136
    • 0002750634 scopus 로고
    • The potential of using cyanobacteria in photobioreactors for hydrogen production
    • Markov, S. A., M. J. Bazin, and D. O. Hall. 1995b. The potential of using cyanobacteria in photobioreactors for hydrogen production. Adv. Biochem. Eng. Biotechnol. 52:61-86.
    • (1995) Adv. Biochem. Eng. Biotechnol. , vol.52 , pp. 61-86
    • Markov, S.A.1    Bazin, M.J.2    Hall, D.O.3
  • 137
    • 0029285984 scopus 로고
    • Hydrogen production and carbon dioxide uptake by immobilised Anabaena variabilis in a hollow fibre photobioreactor
    • Markov, S. A., R. Lichtl, M. J. Bazin, and D. O. Hall. 1995. Hydrogen production and carbon dioxide uptake by immobilised Anabaena variabilis in a hollow fibre photobioreactor. Enzyme Microb. Biotechnol. 17:306-310.
    • (1995) Enzyme Microb. Biotechnol. , vol.17 , pp. 306-310
    • Markov, S.A.1    Lichtl, R.2    Bazin, M.J.3    Hall, D.O.4
  • 138
    • 0030889640 scopus 로고    scopus 로고
    • The heterocyst-specific fdxH gene product of the cyanobacterium Anabaena sp. PCC 7120 is important but not essential for nitrogen fixation
    • Masepohl, B., K. Scholisch, K. Görlitz, C. Kiútski, and H. Böhme. 1997. The heterocyst-specific fdxH gene product of the cyanobacterium Anabaena sp. PCC 7120 is important but not essential for nitrogen fixation. Mol. Gen. Genet. 253:770-776.
    • (1997) Mol. Gen. Genet. , vol.253 , pp. 770-776
    • Masepohl, B.1    Scholisch, K.2    Görlitz, K.3    Kiútski, C.4    Böhme, H.5
  • 139
    • 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. PCC 7120
    • DOI 10.1007/s00253-002-0934-7
    • Masukawa, H., M. Mochimaru, and H. Sakurai. 2002. 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. PCC 7120. Appl. Microbiol. Biotechnol. 58:618-624. (Pubitemid 34302933)
    • (2002) Applied Microbiology and Biotechnology , vol.58 , Issue.5 , pp. 618-624
    • Masukawa, H.1    Mochimaru, M.2    Sakurai, H.3
  • 140
    • 0036836352 scopus 로고    scopus 로고
    • The hydrogenases and photobiological hydrogen production utilizing nitrogenase system in cyanobacteria
    • Masukawa, H., M. Mochimaru, and H. Sakurai. 2002. The hydrogenases and photobiological hydrogen production utilizing nitrogenase system in cyanobacteria. Int. J. Hydrogen Energy 27:1471-1474.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1471-1474
    • Masukawa, H.1    Mochimaru, M.2    Sakurai, H.3
  • 141
    • 63449138662 scopus 로고    scopus 로고
    • Survey of the distribution of different types of nitrogenases and hydrogenases in heterocyst-forming cyanobacteria
    • Masukawa, H., X. Zhang, E. Yamazaki, S. Iwata, K. Nakamura, M. Mochimaru, K. Inoue, and H. Sakurai. 2009. Survey of the distribution of different types of nitrogenases and hydrogenases in heterocyst-forming cyanobacteria. Mar. Biotechnol. 11:397-409.
    • (2009) Mar. Biotechnol. , vol.11 , pp. 397-409
    • Masukawa, H.1    Zhang, X.2    Yamazaki, E.3    Iwata, S.4    Nakamura, K.5    Mochimaru, M.6    Inoue, K.7    Sakurai, H.8
  • 142
    • 0027936189 scopus 로고
    • Mo-independent nitrogenase 3 is advantageous for diazotrophic growth of Azotobacter vinelandii on solid medium containing molydenum
    • Maynard, R. H., R. Premakur, and P. E. Bishop. 1994. Mo-independent nitrogenase 3 is advantageous for diazotrophic growth of Azotobacter vinelandii on solid medium containing molydenum. J. Bacteriol. 176:5583-5586.
    • (1994) J. Bacteriol. , vol.176 , pp. 5583-5586
    • Maynard, R.H.1    Premakur, R.2    Bishop, P.E.3
  • 143
    • 70349527640 scopus 로고    scopus 로고
    • Do toxic cyanobacteria pose a threat to the Baltic ecosystem?
    • Mazur-Marzec, H., and M. Plinski. 2009. Do toxic cyanobacteria pose a threat to the Baltic ecosystem? Oceanologia 51:293-313.
    • (2009) Oceanologia , vol.51 , pp. 293-313
    • Mazur-Marzec, H.1    Plinski, M.2
  • 144
    • 0036193427 scopus 로고    scopus 로고
    • Regulation of cellular differentiation in filamentous cyanobacteria in free-living and plant-associated symbiotic growth states
    • Meeks, J. C., and J. Elhai. 2002. Regulation of cellular differentiation in filamentous cyanobacteria in free-living and plant-associated symbiotic growth states. Microbiol. Mol. Biol. Rev. 66:94-121.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 94-121
    • Meeks, J.C.1    Elhai, J.2
  • 145
    • 0035197070 scopus 로고    scopus 로고
    • Hydrogen production. Green algae as a source of energy
    • Melis, A., and T. Happe. 2001. Hydrogen production. Green algae as a source of energy. Plant Physiol. 127:740-748.
    • (2001) Plant Physiol. , vol.127 , pp. 740-748
    • Melis, A.1    Happe, T.2
  • 146
    • 34247577593 scopus 로고    scopus 로고
    • [FeFe] hydrogenases and their evolution: A genomic perspective
    • Meyer, J. 2007. [FeFe] hydrogenases and their evolution: a genomic perspective. Cell Mol. Life Sci. 64:1063-1084.
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 1063-1084
    • Meyer, J.1
  • 147
    • 0028837420 scopus 로고
    • Mutants of the cyanobacterium Anabaena variabilis altered in hydrogenase activities
    • Mikheeva, L. E., O. Schmitz, S. V. Shestakov, and H. Bothe. 1995. Mutants of the cyanobacterium Anabaena variabilis altered in hydrogenase activities. Z. Naturforsch 50c:505-510.
    • (1995) Z. Naturforsch , vol.50 C , pp. 505-510
    • Mikheeva, L.E.1    Schmitz, O.2    Shestakov, S.V.3    Bothe, H.4
  • 151
    • 0020485044 scopus 로고
    • The pyruvate:ferredoxin oxidoreductase in heterocyts of the cyanobacterium Anabaena cylindrica
    • Neuer, G., and H. Bothe. 1982. The pyruvate:ferredoxin oxidoreductase in heterocyts of the cyanobacterium Anabaena cylindrica. Biochim. Biophys. Acta 716:358-365.
    • (1982) Biochim. Biophys. Acta , vol.716 , pp. 358-365
    • Neuer, G.1    Bothe, H.2
  • 152
    • 53849116782 scopus 로고    scopus 로고
    • The Anabaena sp. strain 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions
    • Neunuebel, M. R., and J. W. Golden. 2008. The Anabaena sp. strain 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions. J. Bacteriol. 190:6829-6838.
    • (2008) J. Bacteriol. , vol.190 , pp. 6829-6838
    • Neunuebel, M.R.1    Golden, J.W.2
  • 153
    • 49649127596 scopus 로고    scopus 로고
    • Physiology, biochemistry and molecular biology of nitrogen fixation
    • H. Bothe, S. J. Ferguson, and W. E. Newton (ed.), Elsevier, Amsterdam, Netherlands
    • Newton, W. E. 2007. Physiology, biochemistry and molecular biology of nitrogen fixation, p. 109-129. In H. Bothe, S. J. Ferguson, and W. E. Newton (ed.), Biology of the nitrogen cycle. Elsevier, Amsterdam, Netherlands.
    • (2007) Biology of the Nitrogen Cycle , pp. 109-129
    • Newton, W.E.1
  • 154
    • 0345478847 scopus 로고
    • Influence of molybdenum, vanadium, and tungsten on growth and nitrogenase synthesis of the free-living cyanobacterium Anabaena azollae
    • Ni, C. V., A. F. Yakuninin, and I. N. Gogotov. 1990. Influence of molybdenum, vanadium, and tungsten on growth and nitrogenase synthesis of the free-living cyanobacterium Anabaena azollae. Microbiology 59:395-398.
    • (1990) Microbiology , vol.59 , pp. 395-398
    • Ni, C.V.1    Yakuninin, A.F.2    Gogotov, I.N.3
  • 155
    • 27744449033 scopus 로고    scopus 로고
    • Functional genomic analysis of three nitrogenase isoenzymes in the photosynthetic bacterium Rhodopseudomonas palustris
    • Oda, Y., S. K. Samanta, F. E. Rey, L. Wu, X. Liu, T. Yan, J. Zhou, and C. S. Harwood. 2005. Functional genomic analysis of three nitrogenase isoenzymes in the photosynthetic bacterium Rhodopseudomonas palustris. J. Bacteriol. 187:7784-7794.
    • (2005) J. Bacteriol. , vol.187 , pp. 7784-7794
    • Oda, Y.1    Samanta, S.K.2    Rey, F.E.3    Wu, L.4    Liu, X.5    Yan, T.6    Zhou, J.7    Harwood, C.S.8
  • 156
    • 65149102920 scopus 로고    scopus 로고
    • Detection of nitrogenase in individual cells of a natural population of Trichodesmium using immunocytochemical methods for fluorescent cells
    • Ohki, K., and Y. Taniuchi. 2009. Detection of nitrogenase in individual cells of a natural population of Trichodesmium using immunocytochemical methods for fluorescent cells. J. Oceanogr. 65:427-432.
    • (2009) J. Oceanogr. , vol.65 , pp. 427-432
    • Ohki, K.1    Taniuchi, Y.2
  • 157
    • 38649135394 scopus 로고    scopus 로고
    • An AbrB-like protein regulates the expression of the bidirectional hydrogenase in Synechocystis sp. strain 6803
    • Oliveira, P., and P. Lindblad. 2008. An AbrB-like protein regulates the expression of the bidirectional hydrogenase in Synechocystis sp. strain 6803. J. Bacteriol. 190:1011-1019.
    • (2008) J. Bacteriol. , vol.190 , pp. 1011-1019
    • Oliveira, P.1    Lindblad, P.2
  • 158
    • 24944525933 scopus 로고    scopus 로고
    • LexA, a transcription regulator binding in the promoter region of the bidirectional hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803
    • DOI 10.1016/j.femsle.2005.07.024, PII S0378109705004854
    • Oliveira, P., and P. Lindblad. 2005. LexA. A transcriptional regulator binding in the promoter region of the bidirectional hydrogenase in the cyanobacterium Synechocystis sp. strain PCC6803. FEMS Microbiol. Lett. 251:59-66. (Pubitemid 41309064)
    • (2005) FEMS Microbiology Letters , vol.251 , Issue.1 , pp. 59-66
    • Oliveira, P.1    Lindblad, P.2
  • 159
    • 72749104137 scopus 로고    scopus 로고
    • Transcriptional regulation of the cyanobacterial Hox-hydrogenase
    • Oliveira, P., and P. Lindblad. 2009. Transcriptional regulation of the cyanobacterial Hox-hydrogenase. Dalton Trans. 45:9990-9996.
    • (2009) Dalton Trans. , vol.45 , pp. 9990-9996
    • Oliveira, P.1    Lindblad, P.2
  • 160
    • 14644427750 scopus 로고    scopus 로고
    • HetR-dependent and -independent expression of heterocyst-related genes in an Anabaena strain overproducing the NtcA transcription factor
    • Olmedo-Verd, E., E. Flores, A. Herrero, and A. M. Muro-Pastor. 2005. HetR-dependent and -independent expression of heterocyst-related genes in an Anabaena strain overproducing the NtcA transcription factor. J. Bacteriol. 187:1985-1991.
    • (2005) J. Bacteriol. , vol.187 , pp. 1985-1991
    • Olmedo-Verd, E.1    Flores, E.2    Herrero, A.3    Muro-Pastor, A.M.4
  • 161
    • 55549087552 scopus 로고    scopus 로고
    • Role of two Ntc-binding sites in the complex ntcA gene promoter of the heterocyst-forming cyanobacterium Anabaena sp. strain 7120
    • Olmedo-Verd, E., A. Valladares, E. Flores, A. Herrero, and A. M. Muro-Pastor. 2008. Role of two Ntc-binding sites in the complex ntcA gene promoter of the heterocyst-forming cyanobacterium Anabaena sp. strain 7120. J. Bacteriol. 190:7584-7590.
    • (2008) J. Bacteriol. , vol.190 , pp. 7584-7590
    • Olmedo-Verd, E.1    Valladares, A.2    Flores, E.3    Herrero, A.4    Muro-Pastor, A.M.5
  • 162
    • 41949139372 scopus 로고    scopus 로고
    • Quantitative shotgun proteomics of enriched heterocysts from Nostoc sp. PCC 7120 using 8-plex isobaric peptide tags
    • Ow, S. Y., T. Cardona, A. Taton, A. Magnuson, P. Lindblad, K. Stensjo, and P. C. Wright. 2008. Quantitative shotgun proteomics of enriched heterocysts from Nostoc sp. PCC 7120 using 8-plex isobaric peptide tags. J. Proteome Res. 7:1615-1626.
    • (2008) J. Proteome Res. , vol.7 , pp. 1615-1626
    • Ow, S.Y.1    Cardona, T.2    Taton, A.3    Magnuson, A.4    Lindblad, P.5    Stensjo, K.6    Wright, P.C.7
  • 165
    • 0020507081 scopus 로고
    • The isocitrate dehydrogenase from cyanobacteria
    • Papen, H., G. Neuer, M. Refaian, and H. Bothe. 1983. The isocitrate dehydrogenase from cyanobacteria. Arch. Microbiol. 134:73-79.
    • (1983) Arch. Microbiol. , vol.134 , pp. 73-79
    • Papen, H.1    Neuer, G.2    Refaian, M.3    Bothe, H.4
  • 166
    • 0022482837 scopus 로고
    • Properties of the glyceraldehyde-3-P dehydrogenase in heterocysts and vegetative cells of cyanobacteria
    • Papen, H., G. Neuer, A. Sauer, and H. Bothe. 1986. Properties of the glyceraldehyde-3-P dehydrogenase in heterocysts and vegetative cells of cyanobacteria. FEMS Microb. Lett. 36:201-206.
    • (1986) FEMS Microb. Lett. , vol.36 , pp. 201-206
    • Papen, H.1    Neuer, G.2    Sauer, A.3    Bothe, H.4
  • 167
    • 0008915393 scopus 로고
    • The alternative nitrogenases
    • M. J. Dilworth and A. R. Glenn (ed.), Elsevier, Amsterdam, Netherlands
    • Pau, R. N. 1991. The alternative nitrogenases, p. 37-57. In M. J. Dilworth and A. R. Glenn (ed.), Biology and biochemistry of nitrogen fixation. Elsevier, Amsterdam, Netherlands.
    • (1991) Biology and Biochemistry of Nitrogen Fixation , pp. 37-57
    • Pau, R.N.1
  • 168
    • 0002625517 scopus 로고    scopus 로고
    • Molydenum transport, processing and gene regulation
    • G. Winkelmann and C. J. Carrano (ed.), Harwood, Newark, NJ
    • Pau, R. N., W. Klipp, and S. Steinkühler. 1997. Molydenum transport, processing and gene regulation, p. 217-234. In G. Winkelmann and C. J. Carrano (ed.), Transition metals in microbial metabolism. Harwood, Newark, NJ.
    • (1997) Transition Metals in Microbial Metabolism , pp. 217-234
    • Pau, R.N.1    Klipp, W.2    Steinkühler, S.3
  • 169
    • 0022656191 scopus 로고
    • The use of Ni to probe the role of hydrogen metabolism in cyanobacterial nitrogen-fixation
    • Pederson, D. M., A. Daday, and G. D. Smith. 1986. The use of Ni to probe the role of hydrogen metabolism in cyanobacterial nitrogen-fixation. Biochimie 68:113-120.
    • (1986) Biochimie , vol.68 , pp. 113-120
    • Pederson, D.M.1    Daday, A.2    Smith, G.D.3
  • 170
    • 45549097973 scopus 로고    scopus 로고
    • A Synechocystis LexA-orthologue binds direct repeats in target genes
    • Petterson-Fortin, L. M., and G. W. Owttrim. 2008. A Synechocystis LexA-orthologue binds direct repeats in target genes. FEBS Lett. 582:2424-2430.
    • (2008) FEBS Lett. , vol.582 , pp. 2424-2430
    • Petterson-Fortin, L.M.1    Owttrim, G.W.2
  • 171
    • 0036174874 scopus 로고    scopus 로고
    • Effects of deletion of genes encoding Fe-only hydrogenase of Desulfovibrio vulgaris Hildenborough on hydrogen and lactate metabolism
    • Pohorelic, B. K. J., J. K. Voordouw, E. Lojou, A. Dolla, J. Harder, and G. Voordouw. 2002. Effects of deletion of genes encoding Fe-only hydrogenase of Desulfovibrio vulgaris Hildenborough on hydrogen and lactate metabolism. J. Bacteriol. 184:679-686.
    • (2002) J. Bacteriol. , vol.184 , pp. 679-686
    • Pohorelic, B.K.J.1    Voordouw, J.K.2    Lojou, E.3    Dolla, A.4    Harder, J.5    Voordouw, G.6
  • 172
    • 33748642375 scopus 로고    scopus 로고
    • Cross functionality of nitrogenase components NifH1 and VnfH in Anabaena variabilis
    • Pratte, B., K. Eplin, and T. Thiel. 2006. Cross functionality of nitrogenase components NifH1 and VnfH in Anabaena variabilis. J. Bacteriol. 188:5806-5811.
    • (2006) J. Bacteriol. , vol.188 , pp. 5806-5811
    • Pratte, B.1    Eplin, K.2    Thiel, T.3
  • 173
    • 3242784266 scopus 로고    scopus 로고
    • Intracellular spheroid bodies of Rhopalodia gibba have nitrogen-fixing apparatus of cyanobacterial origin
    • Prechtl, J., C. Kneip, P. Lockhart, K. Wenderoth, and U.-G. Maier. 2004. Intracellular spheroid bodies of Rhopalodia gibba have nitrogen-fixing apparatus of cyanobacterial origin. Mol. Biol. Evol. 21:1477-1481.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1477-1481
    • Prechtl, J.1    Kneip, C.2    Lockhart, P.3    Wenderoth, K.4    Maier, U.-G.5
  • 175
    • 70349114195 scopus 로고    scopus 로고
    • Characteristics of hydrogen production by immobilized cyanobacterium Microcystis aeruginosa through cycles of photosynthesis and anaerobic incubation
    • Rashid, N., W. Song, J. Park, H. F. Jin, and K. Lee. 2009. Characteristics of hydrogen production by immobilized cyanobacterium Microcystis aeruginosa through cycles of photosynthesis and anaerobic incubation. J. Ind. Eng. Chem. 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
  • 179
    • 0016840118 scopus 로고
    • Interactions among substrates and inhibitors of nitrogenase
    • Rivera-Ortiz, J. M., and R. H. Burris. 1975. Interactions among substrates and inhibitors of nitrogenase. J. Bacteriol. 123:537-545.
    • (1975) J. Bacteriol. , vol.123 , pp. 537-545
    • Rivera-Ortiz, J.M.1    Burris, R.H.2
  • 180
    • 73149085714 scopus 로고    scopus 로고
    • Diversity of total, nitrogen-fixing and denitrifying bacteria in an acid forest soil
    • Rösch, C., and H. Bothe. 2009. Diversity of total, nitrogen-fixing and denitrifying bacteria in an acid forest soil. Eur. J. Soil Sci. 60:883-894.
    • (2009) Eur. J. Soil Sci. , vol.60 , pp. 883-894
    • Rösch, C.1    Bothe, H.2
  • 182
    • 0019161347 scopus 로고
    • Increase of nitrogenase activity in the blue-green alga Nostoc muscorum (cyanobacterium)
    • Scherer, S., W. Kerfin, and P. Böger. 1980. Increase of nitrogenase activity in the blue-green alga Nostoc muscorum (cyanobacterium). J. Bacteriol. 144:1017-1023.
    • (1980) J. Bacteriol. , vol.144 , pp. 1017-1023
    • Scherer, S.1    Kerfin, W.2    Böger, P.3
  • 184
    • 0020069807 scopus 로고
    • Isolation of a hydrogenase-cytochrome b complex from cytoplasmic membarnes of Xanthobacter autotrophicus GZ 29
    • Schink, B. 1982. Isolation of a hydrogenase-cytochrome b complex from cytoplasmic membarnes of Xanthobacter autotrophicus GZ 29. FEMS Microbiol. Lett. 13:289-293.
    • (1982) FEMS Microbiol. Lett. , vol.13 , pp. 289-293
    • Schink, B.1
  • 185
    • 0042201582 scopus 로고
    • Regulatory phenomena in the metabolism of Knallgas bacteria
    • Schlegel, H. G., and U. Eberhardt. 1972. Regulatory phenomena in the metabolism of Knallgas bacteria. Adv. Microbiol. Physiol. 7:205-242.
    • (1972) Adv. Microbiol. Physiol. , vol.7 , pp. 205-242
    • Schlegel, H.G.1    Eberhardt, U.2
  • 186
    • 0034797586 scopus 로고    scopus 로고
    • Quantitative analysis of two circadian clock-controlled gene clusters coding for the birectional hydrogenase in the cyanobacterium Synechoccus sp. PCC7942
    • Schmitz, O., G. Boison, and H. Bothe. 2001. Quantitative analysis of two circadian clock-controlled gene clusters coding for the birectional hydrogenase in the cyanobacterium Synechoccus sp. PCC7942. Mol. Microbiol. 41:1409-1417.
    • (2001) Mol. Microbiol. , vol.41 , pp. 1409-1417
    • Schmitz, O.1    Boison, G.2    Bothe, H.3
  • 188
    • 0037156874 scopus 로고    scopus 로고
    • HoxE - A subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria
    • Schmitz, O., G. Boison, H. Salzmann, H. Bothe, K. Schütz., S. Wang, and T. Happe. 2002. HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria. Biochim. Biophys. Acta 1554:66-74.
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 66-74
    • Schmitz, O.1    Boison, G.2    Salzmann, H.3    Bothe, H.4    Schütz, K.5    Wang, S.6    Happe, T.7
  • 189
    • 0029825520 scopus 로고    scopus 로고
    • The diaphorase subunit HoxU of the bidirectional hydrogenase as electron transferring protein in cyanobacterial respiration?
    • Schmitz, O., and H. Bothe. 1996. The diaphorase subunit HoxU of the bidirectional hydrogenase as electron transferring protein in cyanobacterial respiration? Naturwissenschaften 83:525-527.
    • (1996) Naturwissenschaften , vol.83 , pp. 525-527
    • Schmitz, O.1    Bothe, H.2
  • 190
    • 0030024964 scopus 로고    scopus 로고
    • +-dependent hydrogenase activity in extracts from the cyanobacterium Anacystis nidulans
    • +-dependent hydrogenase activity in extracts from the cyanobacterium Anacystis nidulans. FEMS Microbiol. Lett. 135:97-101.
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 97-101
    • Schmitz, O.1    Bothe, H.2
  • 191
    • 0035808894 scopus 로고    scopus 로고
    • Molecular evidence for the aerobic expression of nifJ, encoding pyruvate:ferredoxin oxidoreductase, in cyanobacteria
    • Schmitz, O., J. Gurke, and H. Bothe. 2001. Molecular evidence for the aerobic expression of nifJ, encoding pyruvate:ferredoxin oxidoreductase, in cyanobacteria. FEMS Microb. Lett. 195:97-102.
    • (2001) FEMS Microb. Lett. , vol.195 , pp. 97-102
    • Schmitz, O.1    Gurke, J.2    Bothe, H.3
  • 192
    • 0027322012 scopus 로고
    • Identification of the nifJ gene coding for pyruvate:ferredoxin oxidoreductase in dinitrogen-fixing cyanobacteria
    • Schmitz, O., T. Kentemich, W. Zimmer, B. Hundeshagen, and H. Bothe. 1993. Identification of the nifJ gene coding for pyruvate:ferredoxin oxidoreductase in dinitrogen-fixing cyanobacteria. Arch. Microbiol. 160:62-67.
    • (1993) Arch. Microbiol. , vol.160 , pp. 62-67
    • Schmitz, O.1    Kentemich, T.2    Zimmer, W.3    Hundeshagen, B.4    Bothe, H.5
  • 193
    • 0028786758 scopus 로고
    • Distinct and differentially regulated Mo-dependent nitrogen-fixing systems evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC 29413: Characterization of the fdX1/2 gene regions as part of the nif1/2 gene clusters
    • Schrautemeier, B., U. Neveling, and S. Schmitz. 1995. Distinct and differentially regulated Mo-dependent nitrogen-fixing systems evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC 29413: characterization of the fdX1/2 gene regions as part of the nif1/2 gene clusters. Mol. Microbiol. 18:357-359.
    • (1995) Mol. Microbiol. , vol.18 , pp. 357-359
    • Schrautemeier, B.1    Neveling, U.2    Schmitz, S.3
  • 195
    • 59349119485 scopus 로고    scopus 로고
    • Immunolocalization of the uptake hydrogenase in the marine cyanobacterium Lyngbya majuscula CCAP 1446/4 and two Nostoc strains
    • Seabra, R., A. Santos, S. Pereira, P. Monades-Ferreira, and P. Tamagnini. 2009. Immunolocalization of the uptake hydrogenase in the marine cyanobacterium Lyngbya majuscula CCAP 1446/4 and two Nostoc strains. FEMS Microbiol. Lett. 292:57-62.
    • (2009) FEMS Microbiol. Lett. , vol.292 , pp. 57-62
    • Seabra, R.1    Santos, A.2    Pereira, S.3    Monades-Ferreira, P.4    Tamagnini, P.5
  • 196
    • 1142275465 scopus 로고    scopus 로고
    • Substrate interactions with nitrogenase: Fe versus Mo
    • Seefeldt, L. C., L. G. Dance, and D. R. Dean. 2004. Substrate interactions with nitrogenase: Fe versus Mo. Biochemistry 43:1401-1409.
    • (2004) Biochemistry , vol.43 , pp. 1401-1409
    • Seefeldt, L.C.1    Dance, L.G.2    Dean, D.R.3
  • 198
    • 36749059000 scopus 로고    scopus 로고
    • In vivo restriction endonuclease activity of the Anabaena PCC 7120 XisA protein in Escherichia coli
    • Shah, G. R., R. Karunakaran, and G. N. Kumar. 2007. In vivo restriction endonuclease activity of the Anabaena PCC 7120 XisA protein in Escherichia coli. Res. Microbiol. 158:679-684.
    • (2007) Res. Microbiol. , vol.158 , pp. 679-684
    • Shah, G.R.1    Karunakaran, R.2    Kumar, G.N.3
  • 199
    • 33751534724 scopus 로고    scopus 로고
    • Genetic control of hydrogen metabolism in cyanobacteria
    • Shestakov, S. V., and L. E. Mikheeva. 2006. Genetic control of hydrogen metabolism in cyanobacteria. Russian J. Genet. 42:1272-1284.
    • (2006) Russian J. Genet. , vol.42 , pp. 1272-1284
    • Shestakov, S.V.1    Mikheeva, L.E.2
  • 200
    • 33746583497 scopus 로고    scopus 로고
    • Regulation of intracellular free calcium concentration during heterocyst differentiation by HetR and NtcA in Anabaena sp PCC 7120
    • Shi, Y. M., W. X. Zhao, W. Zhang, Z. Ye, and J. D. Zhao. 2006. Regulation of intracellular free calcium concentration during heterocyst differentiation by HetR and NtcA in Anabaena sp PCC 7120. Proc. Natl. Acad. Sci. U. S. A. 103:11334-11339.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11334-11339
    • Shi, Y.M.1    Zhao, W.X.2    Zhang, W.3    Ye, Z.4    Zhao, J.D.5
  • 202
    • 27644449352 scopus 로고    scopus 로고
    • Quantitative analysis of nifH genes and transcripts from aquatic environments
    • Short, S. M., and J. P. Zehr. 2005. Quantitative analysis of nifH genes and transcripts from aquatic environments. Methods Enzymol. 397:380-394.
    • (2005) Methods Enzymol. , vol.397 , pp. 380-394
    • Short, S.M.1    Zehr, J.P.2
  • 203
    • 0021757851 scopus 로고
    • A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase
    • Simpson, F. B., and R. H. Burris. 1984. A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase. Science 224:105-1097.
    • (1984) Science , vol.224 , pp. 105-1097
    • Simpson, F.B.1    Burris, R.H.2
  • 205
    • 0017182745 scopus 로고
    • Inhibition by acetylene of conventional hydrogenase in nitogen-fixing bacteria
    • Smith, L. A., S. Hill, and M. G. Yates. 1976. Inhibition by acetylene of conventional hydrogenase in nitogen-fixing bacteria. Nature 262:209-210.
    • (1976) Nature , vol.262 , pp. 209-210
    • Smith, L.A.1    Hill, S.2    Yates, M.G.3
  • 206
    • 67650001309 scopus 로고    scopus 로고
    • Is the distribution of nitrogen-fixing cyanobacteria in the oceans related to temperature?
    • Stal, L. J. 2009. Is the distribution of nitrogen-fixing cyanobacteria in the oceans related to temperature? Environ. Mirobiol. 11:1632-1645.
    • (2009) Environ. Mirobiol. , vol.11 , pp. 1632-1645
    • Stal, L.J.1
  • 207
    • 0030669394 scopus 로고    scopus 로고
    • Fermentation in cyanobacteria
    • Stal, L. J., and R. Mozelaar. 1997. Fermentation in cyanobacteria. FEMS Microbiol. Rev. 21:179-211.
    • (1997) FEMS Microbiol. Rev. , vol.21 , pp. 179-211
    • Stal, L.J.1    Mozelaar, R.2
  • 208
    • 0017324410 scopus 로고
    • Phototrophic prokaryotes: The cyanobacteria
    • Stanier, R. Y., and G. Cohen-Bazire. 1977. Phototrophic prokaryotes: the cyanobacteria. Annu. Rev. Microbiol. 31:225-274.
    • (1977) Annu. Rev. Microbiol. , vol.31 , pp. 225-274
    • Stanier, R.Y.1    Cohen-Bazire, G.2
  • 209
    • 0014897841 scopus 로고
    • Nitrogenase activity in the blue-green alga Plectonema boryanum
    • Stewart, W. D. P., and M. Lex. 1970. Nitrogenase activity in the blue-green alga Plectonema boryanum. Archiv. Mikrob. 73:250-260.
    • (1970) Archiv. Mikrob. , vol.73 , pp. 250-260
    • Stewart, W.D.P.1    Lex, M.2
  • 210
    • 72749090095 scopus 로고    scopus 로고
    • How algae produce hydrogen - News from the photosynthetic hydrognase
    • Stripp, S. T., and T. Happe. 2009. How algae produce hydrogen - news from the photosynthetic hydrognase. Dalton Trans. 45:9960-9969.
    • (2009) Dalton Trans. , vol.45 , pp. 9960-9969
    • Stripp, S.T.1    Happe, T.2
  • 216
    • 0027495919 scopus 로고
    • Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis
    • Thiel, T. 1993. Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis. J. Bacteriol. 175:6276-6286.
    • (1993) J. Bacteriol. , vol.175 , pp. 6276-6286
    • Thiel, T.1
  • 217
    • 0029049235 scopus 로고
    • A second nitrogenase in vegetative cells of a heterocyst-forming cyanobacterium
    • Thiel, T., E. M. Lyons, J. Erker, and A. Ernst. 1995. A second nitrogenase in vegetative cells of a heterocyst-forming cyanobacterium. Proc. Natl. Acad. Sci. U. S. A. 92:9358-9362.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9358-9362
    • Thiel, T.1    Lyons, E.M.2    Erker, J.3    Ernst, A.4
  • 218
    • 33845336120 scopus 로고    scopus 로고
    • A second isoform of ferredoxin:NADP oxidoreductase generated by an in-frame initiation of translation
    • Thomas, J.-C., B. Ughy, B. Lagoutte, and G. Ajlani. 2006. A second isoform of ferredoxin:NADP oxidoreductase generated by an in-frame initiation of translation. Proc. Natl. Acad. Sci. U. S. A. 103:18368-18373.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18368-18373
    • Thomas, J.-C.1    Ughy, B.2    Lagoutte, B.3    Ajlani, G.4
  • 220
    • 0001442098 scopus 로고
    • Kinetics and mechanism of the nitrogenase enzyme system
    • T. Spiro (ed.), J. Wiley, New York, NY
    • Thorneley, R. N. F., and D. J. Lowe. 1985. Kinetics and mechanism of the nitrogenase enzyme system, p. 222-284. In T. Spiro (ed.), Molydenum enzymes. J. Wiley, New York, NY.
    • (1985) Molydenum Enzymes , pp. 222-284
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 221
    • 84989997759 scopus 로고
    • Zur Rolle des Phytoflavins im photosynthetischen Elektronentransport
    • Trebst, A., and H. Bothe. 1966. Zur Rolle des Phytoflavins im photosynthetischen Elektronentransport. Ber. Dtsch. Bot. Ges. 79:44-47.
    • (1966) Ber. Dtsch. Bot. Ges. , vol.79 , pp. 44-47
    • Trebst, A.1    Bothe, H.2
  • 222
    • 34249687026 scopus 로고    scopus 로고
    • Nitrogen fixing cyanobacteria: A review
    • Tsygankov, A. 2007. Nitrogen fixing cyanobacteria: a review. Appl. Biochem. Microbiol. 43:250-259.
    • (2007) Appl. Biochem. Microbiol. , vol.43 , pp. 250-259
    • Tsygankov, A.1
  • 223
    • 51549091583 scopus 로고    scopus 로고
    • Transcription activation by NtcA and 2-oxoglutarate of three genes involved in heterocyst differentiation in the cyanobacterium Anabaena sp. strain PCC 7120
    • Valladares, A., E. Flores, and A. Herrero. 2008. Transcription activation by NtcA and 2-oxoglutarate of three genes involved in heterocyst differentiation in the cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 190:126-6133.
    • (2008) J. Bacteriol. , vol.190 , pp. 126-6133
    • Valladares, A.1    Flores, E.2    Herrero, A.3
  • 225
    • 0015267120 scopus 로고
    • Flavodoxin from Azotobacter vinelandii
    • Van Lin, B., and H. Bothe. 1972. Flavodoxin from Azotobacter vinelandii. Arch. Microbiol. 82:155-172.
    • (1972) Arch. Microbiol. , vol.82 , pp. 155-172
    • Van Lin, B.1    Bothe, H.2
  • 226
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification and biological function of hydrogenases: An overview
    • Vignais, P. M., and B. Billoud. 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
  • 227
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P. M., B. Billoud, and J. Meyer. 2001. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25:455-501.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 228
    • 2142653130 scopus 로고    scopus 로고
    • Molecular biology of microbial hydrogenases
    • Vignais, P. M., and A. Colbeau. 2004. Molecular biology of microbial hydrogenases. Curr. Issues Mol. Biol. 6:159-188.
    • (2004) Curr. Issues Mol. Biol. , vol.6 , pp. 159-188
    • Vignais, P.M.1    Colbeau, A.2
  • 229
    • 36649021300 scopus 로고    scopus 로고
    • The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases
    • Vogt, S., E. J. Lyon, S. Shima, and R. K. Thauer. 2008. The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases. J. Biol. Inorg. Chem. 13:97-106.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 97-106
    • Vogt, S.1    Lyon, E.J.2    Shima, S.3    Thauer, R.K.4
  • 230
    • 34547174733 scopus 로고    scopus 로고
    • Cyanobacterial heterocysts. Terminal pores proposed as sites of gas exchange
    • Walsby, A. E. 2007. Cyanobacterial heterocysts. terminal pores proposed as sites of gas exchange. Trends Microbiol. 15:340-349.
    • (2007) Trends Microbiol. , vol.15 , pp. 340-349
    • Walsby, A.E.1
  • 231
    • 42049094614 scopus 로고    scopus 로고
    • Transcription of hupSL in Anabaena variabilis ATTC 29143 is regulated by NtcA and not by hydrogen
    • Weyman, P. D., B. Pratte, and T. Thiel. 2008. Transcription of hupSL in Anabaena variabilis ATTC 29143 is regulated by NtcA and not by hydrogen. Appl. Environ. Microbiol. 74:2103-2110.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 2103-2110
    • Weyman, P.D.1    Pratte, B.2    Thiel, T.3
  • 233
    • 3042611448 scopus 로고    scopus 로고
    • Presence and expression of hydrogenase specific C-terminal endopeptidases in cyanobacteria
    • Wünschiers, R., M. Batur, and P. Lindblad. 2003. Presence and expression of hydrogenase specific C-terminal endopeptidases in cyanobacteria. BMC Microbiol. 3:8-20.
    • (2003) BMC Microbiol. , vol.3 , pp. 8-20
    • Wünschiers, R.1    Batur, M.2    Lindblad, P.3
  • 234
    • 25144493215 scopus 로고    scopus 로고
    • The interstitial atom of the nitrogenase FeMo-cofactor: Endor and ESEEM evidence that it is not a nitrogen
    • Yang, T., N. Maeser, M. Laryukhin, H. I. Lee, D. R. Daen, L. C. Seefeldt, and B. M. Hoffman. 2005. The interstitial atom of the nitrogenase FeMo-cofactor: Endor and ESEEM evidence that it is not a nitrogen. J. Am. Chem. Soc. 127:12804-12805.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12804-12805
    • Yang, T.1    Maeser, N.2    Laryukhin, M.3    Lee, H.I.4    Daen, D.R.5    Seefeldt, L.C.6    Hoffman, B.M.7
  • 235
    • 1842342057 scopus 로고
    • Electron-transport to nitrogenase in Azotobacter chroococcum - Azotobacter flavodoxin hydroquinone as an electron donor
    • Yates, M. G. 1972. Electron-transport to nitrogenase in Azotobacter chroococcum - Azotobacter flavodoxin hydroquinone as an electron donor. FEBS Lett. 27:63-67.
    • (1972) FEBS Lett. , vol.27 , pp. 63-67
    • Yates, M.G.1
  • 236
    • 0032582692 scopus 로고    scopus 로고
    • Heterocyst pattern formation controlled by a diffusible peptide
    • Yoon, H. S., and J. W. Golden. 1998. Heterocyst pattern formation controlled by a diffusible peptide. Science 282:935-938.
    • (1998) Science , vol.282 , pp. 935-938
    • Yoon, H.S.1    Golden, J.W.2
  • 239
    • 30744452739 scopus 로고    scopus 로고
    • Heterocyst differentiation and pattern formation in cyanobacteria. A chorus of signals
    • Zhang, C. C., S. Laurent, S. Sakr, L. Peng, and S. Bedu. 2006. Heterocyst differentiation and pattern formation in cyanobacteria. a chorus of signals. Mol. Microb. 59:367-375.
    • (2006) Mol. Microb. , vol.59 , pp. 367-375
    • Zhang, C.C.1    Laurent, S.2    Sakr, S.3    Peng, L.4    Bedu, S.5
  • 240
    • 36348936871 scopus 로고    scopus 로고
    • PII is important in regulation of nitrogen metabolism but not required for heterocyst formation in the cyanobacterium Anabaena sp PCC 7120
    • Zhang, C. C., H. Pu, Q. S. Wang, S. Cheng, W. X. Zhao, Y. Zhang, and J. D. Zhao. 2007. PII is important in regulation of nitrogen metabolism but not required for heterocyst formation in the cyanobacterium Anabaena sp PCC 7120. J. Biol. Chem. 282:33641-33648.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33641-33648
    • Zhang, C.C.1    Pu, H.2    Wang, Q.S.3    Cheng, S.4    Zhao, W.X.5    Zhang, Y.6    Zhao, J.D.7
  • 241
    • 48549092471 scopus 로고    scopus 로고
    • Gene expression patterns of sulfur starvation in Synechocystis sp. PCC 6803
    • Zhang, Z., N. D. Pendse, K. N. Phillips, J. B. Cotner, and A. Khodursky. 2008. Gene expression patterns of sulfur starvation in Synechocystis sp. PCC 6803. BMC Genomics 9:344-354.
    • (2008) BMC Genomics , vol.9 , pp. 344-354
    • Zhang, Z.1    Pendse, N.D.2    Phillips, K.N.3    Cotner, J.B.4    Khodursky, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.