Nitrogen Fixation: From Molecules to Crop Productivity: Proceedings of the 12th International Congress on Nitrogen Fixation, Foz Do Iguaçu, Paraná, Br

ISBN-13: 9780792362333 / Angielski / Twarda / 2000 / 669 str.

Geoffrey Yates; Fabio O. Pedrosa; Mariangela Hungria

Opis

The 12th International Congress on Nitrogen Fixation was held in Foz do Iguacu, Parana State, Brazil, from the 12th to 17th of September, 1999. This volume constitutes the proceedings of this Congress and represents a compilation of the presentations by scientists from 38 countries who came to discuss the progress made, to exchange views and to collaborate. Since the first meeting in Pullman, Washington, USA, in 1974, this series of Congresses has been held three times in the United States, four times in Western Europe, in Australia, Mexico and Russia, and now for the first time in South America. Brazil was a most appropriate choice because Brazilian agriculture is especially dependent on biological nitrogenfixation. An important example is the soybean crop. The 30 million metric tons of grain produced each year relies solely on symbiotic nitrogen fixation. N-fertilizers are expensive in Brazil and, in the absence of the biological process, this crop would require 4-5 M tonnes of N at an annual cost of almost 1 billion dollars. Crop rotation, soil reclamation, forestry, forage mixed cropping, intercropping with grasses and legumes, associative nitrogen fixation with non-legume crops, such as sugarcane, and other agricultural practices in Brazil are also dependent on biological nitrogen fixation. The Brazilian experience with biological nitrogen fixation is a paradigm to be followed by all countries where nitrogen fertiliser is expensive or where present day environmental concerns demand a feasible, efficient and inexpensive alternative to chemical N-fertilizers.

Spis treści

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