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Anabaena cyanobacterium

Figure 1. Left Anatoxin-a (ANTX-A) hydrochloride. Produced by the freshwater filamentous cyanobacterium Anabaena flos-aquae NRC-44-1. Right Anatoxin-a(s). Produced by the freshwater filamentous cyanobacterium Anabaena flos-aquae NRC-525-17. Bottom Aphantoxin-I (neosaxitoxin) and Aphantoxin-II (saxitoxin) produced by certain strains of the filamentous cyanobacterium Aphantomenon flos-aquae. Figure 1. Left Anatoxin-a (ANTX-A) hydrochloride. Produced by the freshwater filamentous cyanobacterium Anabaena flos-aquae NRC-44-1. Right Anatoxin-a(s). Produced by the freshwater filamentous cyanobacterium Anabaena flos-aquae NRC-525-17. Bottom Aphantoxin-I (neosaxitoxin) and Aphantoxin-II (saxitoxin) produced by certain strains of the filamentous cyanobacterium Aphantomenon flos-aquae.
Kuritz T, LV Bocanera, NS Rivera (1997) Dechlorination of lindane by the cyanobacterium Anabaena sp. [Pg.84]

G. D. Smith, G. R. Lambert (1981) An outdoor biophotolytic system using the cyanobacterium Anabaena cylindrica B629. Biotechnol. Bioeng., 23 213-220... [Pg.69]

T. Happe, K. Schiitz, H. Bohm (2000) Transcriptional and mutational analysis of the uptake hydrogenase of the filamentous cyanobacterium Anabaena variabilis ATCC 29413.. /. Bacteriology, 182 1624-1631... [Pg.81]

T. Thiel (1993) Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis. J. Bacteriol., 175 6276-6286... [Pg.91]

T. Kaneko.Y. Nakamura, CP. Wolk, T. Kuritz, S. Sasamoto, A. Watanabe, M. Iriguchi, A. Ishikawa, K. Kawashima, T. Kimura, Y. Kishida, M. Kohara, M. Matsumoto, A. Matsuno, A. Muraki, N. Nakazaki, S. Shimpo, M. Sugimoto.M. Takazawa, M. Yamada, M. Yasuda, S. Tabata (2001) Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNARes, 8 205-213... [Pg.92]

Onodera H, Oshima Y, Henriksen P, Yasumoto T (1997) Confirmation of anatoxin-a(s) in the cyanobacterium Anabaena lemmermanni as the cause of bird kills in Danish lakes. Toxicon 35 1645-1648... [Pg.118]

Ewart, G. D. and Smith, G. D. (1989) Purification and properties of soluble hydrogenase from the cyanobacterium Anabaena cylindrical. Arch. Biochem. Biophys., 268, 327-37. [Pg.262]

Golden, J. W., Robinson, S. J. and Haselkorn, R. (1985) Rearrangement of nitrogen fixation genes during heterocyst differentiation in the cyanobacterium Anabaena. Nature, 314, 419-23. [Pg.264]

Matveyev, A. V., Rutgers, E., Soderhack, E. and Bergman, B. (1994) A novel rearrangement involved in heterocyst differentiation of the cyanobacterium Anabaena sp. PCC7120. FEMS Microbiol. Lett., 116, 201-8. [Pg.270]

Although apparently derived from the bacterial two-component signaling system, the ethylene system in Arabidopsis is different in that the His kinase activity that defines component 1 in bacteria is not essential to the transduction in Arabidopsis. The genome of the cyanobacterium Anabaena encodes proteins with both an ethylene-binding domain and an active His kinase domain. It seems likely that in the course of evolution, the ethylene receptor of vascular plants was derived from that of a cyanobacterial endosymbiont, and that the bacterial His kinase became a Ser/Thr kinase in the plant. [Pg.454]

FIGURE 19-5 Iron-sulfur centers. The Fe-S centers of iron-sulfur proteins may be as simple as (a), with a single Fe ion surrounded by the S atoms of four Cys residues. Other centers include both inorganic and Cys S atoms, as in (b) 2Fe-2S or (c) 4Fe-4S centers, (d) The ferredoxin of the cyanobacterium Anabaena 7120 has one 2Fe-2S center (PDB ID 1 FRD) Fe is red, inorganic S2 is yellow, and the S of Cys is orange. (Note that in these designations only the inorganic S atoms are counted. For example, in the 2Fe-2S center (b), each Fe ion is actually surrounded by four S atoms.) The exact standard reduction potential of the iron in these centers depends on the type of center and its interaction with the associated protein. [Pg.695]

Figure 23-24 (A) Stereoscopic view of a hexameric (a(3)3 phycobiliprotein. (B) The (3 subunit of the complex with two molecules of bound phyco-ery throbilin and one of phy-courobilin. From Chang et al.279 (C) Schematic representation of a phycobilosome of a strain of the cyanobacterium Anabaena. Each disk in the structure contains an (a(3)3 phycobiliprotein. The circles marked AP are cross-sections of rods, each one composed of about four disks of allophycocyanin (AP). Figure 23-24 (A) Stereoscopic view of a hexameric (a(3)3 phycobiliprotein. (B) The (3 subunit of the complex with two molecules of bound phyco-ery throbilin and one of phy-courobilin. From Chang et al.279 (C) Schematic representation of a phycobilosome of a strain of the cyanobacterium Anabaena. Each disk in the structure contains an (a(3)3 phycobiliprotein. The circles marked AP are cross-sections of rods, each one composed of about four disks of allophycocyanin (AP).
L.E. Llewellyn, A.P. Negri, J. Doyle, P.D. Baker, E.C. Beltran and B.A. Neilan, Radioreceptor assays for sensitive detection and quantitation of saxitoxin and its analogues from strains of the freshwater cyanobacterium, Anabaena circinalis, Environ. Sci. Technol., 35 (2001) 1445-1451. [Pg.352]

Subramonian, G. and Shanmugaundaram, S. 1986. Uninduced ammonia release by the nitrogen fixing cyanobacterium Anabaena. FEMS Microbiology Letters, 37,151-154. [Pg.32]

Charng. Y.-Y.. Kakefuda, G., Iglesisas. A. A.. Buikema, W. J., and Preiss, J. 1992. Molecular cloning and expression of the gene encoding ADP-glucose pyrophosphorylase from cyanobacterium Anabaena sp. strain PCC 7120, Plant Mol. Biol. 20, 37-47. [Pg.174]

Kentemich, T., Danneberg, G., Hundeshagen, B., and Bothe, H. 1988. Evidence for the occurrence of the alternative, vanadium-containing nitrogenase in the cyanobacterium Anabaena variabilis. FENS Microbiol. Lett. 51, 19-24. [Pg.262]

Thiel, T., and Pratte, B. 2001. Effect of heterocyst differentiation of nitrogen fixation in vegetative cells of the cyanobacterium Anabaena variabilis ATCC 29413. J. Bacteriol. 183, 280-286. [Pg.269]

Anatoxin-A (S), an anticholinesterase from the cyanobacterium Anabaena flos-aquae NRC-525-17. Toxicon... [Pg.156]

Moreno, J., Vargas, M.A., Rodriguez, H., Rivas, J., Guerrero, M.G. (2003). Outdoor cultivation of nitrogen-fixing marine cyanobacterium, Anabaena ATCC 33047. Biomolec. Eng. 20 191-7. [Pg.378]

Negri, A.P., Jones, G.J. (1995). Bioaccumulation of paralytic shellfish poisoning (PSP) toxins Ifom the cyanobacterium Anabaena circinalis by the freshwater mussel Alathyria con-dola. Toxicon 33 667-78. [Pg.378]

Buikema, W. J., and Haselkom, R. (1991). Characterization of a gene controlling heterocyst differentiation in the cyanobacterium Anabaena 7120. Genes Dev. 5, 321-330. [Pg.1214]


See other pages where Anabaena cyanobacterium is mentioned: [Pg.80]    [Pg.81]    [Pg.91]    [Pg.118]    [Pg.54]    [Pg.226]    [Pg.267]    [Pg.174]    [Pg.70]    [Pg.108]    [Pg.182]    [Pg.473]    [Pg.1324]    [Pg.167]    [Pg.233]    [Pg.156]    [Pg.236]    [Pg.242]    [Pg.264]    [Pg.142]    [Pg.1558]   
See also in sourсe #XX -- [ Pg.211 ]




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