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Nitrogen Fixation: From Molecules to Crop Productivity, Softcover reprint of the original 1st ed. 2002 Proceedings of the 12th International Congress on Nitrogen Fixation, Foz do Iguaçu, Paraná, Brazil, September 12-17, 1999 Current Plant Science and Biotechnology in Agriculture Series, Vol. 38

Langue : Anglais

Coordonnateurs : Pedrosa Fabio O., Hungria Mariangela, Yates Geoffrey, Newton William E.

Couverture de l’ouvrage Nitrogen Fixation: From Molecules to Crop Productivity

These proceedings bring together diverse disciplines that study nitrogen fixation and describe the most recent advances made in various fields: chemists are now studying FeMoco, the active site of nitrogenase in non-protein surroundings, and have refined the crystal structure of the enzyme to 1.6 angstroms.

Keynote Lecture. Nitrogen fixation in perspective; W.E. Newton. Section I: Biochemistry and Chemistry. Chemistry and biochemistry of nitrogenase; B.E. Smith. The mechanism of molybdenum nitrogenase: An overview; B.K. Burgess. Roles for nucleotides in nitrogenase catalysis; L.C. Seefeldt, et al. Superoxide-dependent nitrogen fixation; C. Hofmann-Findeklee, et al. Chemistry and biochemistry of nitrogenase (Part 1); R.N.F. Thorneley, et al. A 1.6 A resolution x-ray crystallographic study of Klebsiella pneumoniae MoFe protein, Kp1; S.M. Mayer, et al. Roles of VnfX and NifX in FeV-co and FeMo-co synthesis in Azotobacter vinelandii; C. Rüttimann-Johnson, et al. Studies on the mechanism for the activiation of iron and sulfur for formation of the nitrogenase metal centers; D.R. Dean, et al. Stopped-flow infra-red spectroscopy of carbon monoxide binding to functioning nitrogenase; R.N.F. Thorneley, et al. Reductant-dependent ATP utilization during nitrogenase catalysis: Studies using Ti (III); A.C. Nyborg, et al. Cofactor reactivity and models for cofactor reactions; G.J. Leigh, R.L. Richards. Interactions of small molecules with isolated FeMoco; C.J. Pickett, et al. Catalytic reactions with FeMoco in non-enzymatic surroundings (comparison with synthetic catalysts); A.E. Shilov. Catalytic behavior of isolated FeMo-cofactor of nitrogenase in non-protein surroundings; T.A. Bazhenova, et al. Chemical nitrogen fixation: protonation of coordinated dinitrogen with coordinated dihydrogen or bridging hydrosulfido ligands; M. Hidai. Mo, V and Fe complexes of tripodal sulfur-donor ligands as models for nitrogenase active sites; S.C. Davies, et al. The use of chemicals models to probe the mechanisms of substrate reduction reactions of nitrogenases; C.A. Helleren, etal. Poster Summaries. Section II: Regulation of Nitrogen Fixation and Assimilation. Regulation of nif gene expression in free-living diazotrophs: recent advances; M.J. Merrick, et al. Activation of transcription by the sigma-54 RNA polymerase holoenzyme; M.-T. Gallegos, et al. New mechanisms of bacterial gene regulation in a nitrogen-fixing phototroph; R.G. Kranz, et al. Regulation of nitrogen fixation and glutamine synthetase in Herbaspirillum seropedicae; E.M. Souza, et al. Analysis of bacterial gene expression during the late stages of the interaction between Rhizobium etli CNPAF512 and Phaseolus vulgaris; J. Michiels, et al. Functional analysis of the Bradyrhizobium japonicum RegSR two-component regulatory proteins; R. Emmerich, et al. Role of Herbaspirillum seropedicae NifA domains on the expression of nif genes; R.A. Monteiro, et al. Characterization of an Azospirillum brasilense Tn5 mutant with enhanced nitrogen fixation; C.A.G. Blaha, et al. amtB is necessary for NH4+ induced nitrogenase switch-off and ADP-ribosylation in Rhodobacter capculatus; A.F. Yakunin, P.C. Hallenbeck. Regulation of Azotobacter vinelandii NifA activity by NifL: Role of PII-like proteins in nitrogen sensing; F. Reyes-Ramirez, et al. Structural basis for signal transduction within the FixJ transcriptional activator; J. Schumacher, et al. Effect of redox status of dinitrogenase reductase on the regulation of nitrogenase activity by reversible ADP-ribosylation; C.M. Halbleib, et al. Heterotrimerization of PII-like signalling proteins: Lessons from a comparative analysis between a cyanobacterial PII homologue and its proteobacterial cou

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Date de parution :

Ouvrage de 669 p.

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Prix indicatif 316,49 €

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