Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Ferredoxins Anabaena

Fig. 9. Cysteine residues involved in the Cys-to-Ser substitutions carried out on [2Fe-2S] proteins. The reducible site of the center was identified by NMR in the case oi Anabaena ferredoxin (42). Fig. 9. Cysteine residues involved in the Cys-to-Ser substitutions carried out on [2Fe-2S] proteins. The reducible site of the center was identified by NMR in the case oi Anabaena ferredoxin (42).
Amyotrophic lateral sclerosis (ALS), peroxyni-trite implicated, 46 402 Anabaena, heterocyst ferredoxin, 38 229 Anabaena sphaeria, ferredoxins, 38 228-229 Anaerobic controlled potential electrolysis, Azotobacter, 38 129... [Pg.11]

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 2.30. Ferredoxin from the cyanobacterium Anabaena PCC 7119. Each branch has an Fe2S2 cluster. Proteins are shown schematically as ribbons, and side chains are shown as atoms. Surrounding dots are oxygen atoms from water molecules (hydrogens not shown). Based on Protein Data Bank ID ICZP (Morales et ah, 1999). Figure 2.30. Ferredoxin from the cyanobacterium Anabaena PCC 7119. Each branch has an Fe2S2 cluster. Proteins are shown schematically as ribbons, and side chains are shown as atoms. Surrounding dots are oxygen atoms from water molecules (hydrogens not shown). Based on Protein Data Bank ID ICZP (Morales et ah, 1999).
Mulligan, M.E., Buikema, W.J. and Haselkom, R. (1988). Bacterial-type ferredoxin genes in the nitrogen fixation regions of the cyanobacterium Anabaena sp. strain PCC 7120 and Rhizobium meliloti. J. Bacteriol. 170,4406-4410. [Pg.166]

Fig. 15. Three-dimensional structure of Anabaena ferredoxin in ribbon representation. The five strands of p-pleated sheet are labeled A to E. Figure source Holden, Jackson, Jacobson, Hurley, Tollin, Oh, Skjedal, Chae, Cheng, Xia and Markley (1993) Structure-function studies of[2Fe-2S] ferredoxins. J Bioenerg Biomembr 26 72. Fig. 15. Three-dimensional structure of Anabaena ferredoxin in ribbon representation. The five strands of p-pleated sheet are labeled A to E. Figure source Holden, Jackson, Jacobson, Hurley, Tollin, Oh, Skjedal, Chae, Cheng, Xia and Markley (1993) Structure-function studies of[2Fe-2S] ferredoxins. J Bioenerg Biomembr 26 72.
Anusevicius Z et al., Electron transferreactions of Anabaena PCC 7119 ferredoxin NADP+ reductase with nonphysiological antioxidants, Biochim. Biophys. Acta, 1320, 247, 1997. [Pg.224]

X-ray structure of the ferredoxin NADP-l-reduetase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP binding at 2.25 A resolution. J. Mol. Biol 263, 20-39. [Pg.141]

Curdt, L, Singh, B.B., Jakoby, M., Hachtel, W., and Bohme, H. (2000). Identification of amino acid residues of nitrite reductase from Anabaena sp. PCC 7120 involved in ferredoxin binding. Biochim. Biophys. Acta 1543, 60-68. [Pg.130]

IMMUNOCYTOCHEMICAL LOCALIZATION OF THE ELECTRON CARRIER PROTEINS FERREDOXIN-NADP+OXIDOREDUCTASE AND CYTOCHROME c553 IN THE N2-FIXING CYANOBACTERIUM Anabaena variabilis... [Pg.2866]

Immunocytochemical Localization of the Electron Carrier Proteins Ferredoxin-NADP+Oxidoreductase and Cytochrome c 553 in the N2-Fixing Cyanobacterium Anabaena variabilis 95... [Pg.3838]

Similarly, for 2Fe(2-,3-) clusters in protein environments, the redox shift between Anabaena ferredoxin (a single domain protein) and phthalate dioxygenase reductase (PDR, a three-domain protein which is reasonably homologous in the first domain) was reasonably reproduced PDR has a more positive potential by about 0.2 eV and the theoretical shift prediction is close to this, whether by a single cycle Poisson-Boltzmann calculation or with more elaborate SCRF methodology. This redox shift can be traced mainly to one additional strong N—H—S hydrogen bond... [Pg.507]

Assimilatory N.r. from bacteria (Azolobacier chroococcum, Ectothiorhodospira shaposhnikovU) and cyanobacteria (Anabaena cylindrica, Anacyslis nidulans) are specific for reduced ferredoxin, and they do not react with NAD(P)H. [Pg.433]

FIGURE 134.2 Stereoscopic views of ferredoxin (A) and FNR (B) of Anabaena PCC 7119 showing the positions of key amino acid residues that are critical for molecular recognition. (From Gomez-Moreno, C., Martinez-Julvez, M., Fillat, M.F., Hurley, J.K., and Tollin, G., Biochem. Soc. Trans., 24, 111, 1996. With permission.)... [Pg.2613]

Apte, SK, Rowell p and Stewart WDP (1978) Electron donation to ferredoxin in heterocysts of the N2-fixing alga Anabaena cylindrica, Proc. R. Soc. Lond. B 200, 1-25. [Pg.713]


See other pages where Ferredoxins Anabaena is mentioned: [Pg.452]    [Pg.453]    [Pg.455]    [Pg.455]    [Pg.70]    [Pg.1324]    [Pg.236]    [Pg.622]    [Pg.236]    [Pg.695]    [Pg.390]    [Pg.44]    [Pg.310]    [Pg.1620]    [Pg.1647]    [Pg.2866]    [Pg.2946]    [Pg.508]    [Pg.208]    [Pg.87]    [Pg.229]    [Pg.230]    [Pg.713]   
See also in sourсe #XX -- [ Pg.455 ]




SEARCH



Ferredoxins

© 2024 chempedia.info