Purification and characterization of the nifN and nifE gene products from Azotobacter vinelandii mutant UW45.
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Purification and characterization of the nifN and nifE gene products from Azotobacter vinelandii mutant UW45.
The nifN and -E gene products are involved in the synthesis of the iron-molybdenum cofactor of dinitrogenase, the enzyme responsible for the reduction of dinitrogen to ammonia. By using the in vitro iron-molybdenum cofactor biosynthesis assay, we have followed the purification of these gene products 450-fold to greater than 95% purity. An overall recovery of 20% was obtained with the purified p...
متن کاملPurification and Characterization of NafY (Apodinitrogenase Subunit) from Azotobacter vinelandii*
The formation of an active dinitrogenase requires the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized apodinitrogenase. In Azotobacter vinelandii, NafY (also known as protein) has been proposed to be a FeMo-co insertase because of its ability to bind FeMo-co and apodinitrogenase. Here we report the purification and biochemical characterization of NafY...
متن کاملIn vitro synthesis of the iron-molybdenum cofactor of nitrogenase.
Molybdate- and ATP-dependent in vitro synthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase requires the protein products of at least the nifB, nifN, and nifE genes. Extracts of FeMo-co-negative mutants of Klebsiella pneumoniae and Azotobacter vinelandii with lesions in different genes can be complemented for FeMo-co synthesis. Both K. pneumoniae and A. vinelandii dinitrogenase (co...
متن کاملPurification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii.
1. A soluble reduced Methyl Viologen-dependent assimilatory nitrate reductase from Azotobacter vinelandii strain UW136 grown aerobically on nitrate was purified to homogeneity by the criteria of nitrate reductase activity staining, and coincidence of a Coomassie Blue-staining protein band on polyacrylamide gels run under non-denaturing conditions. The specific activity was 3 mumol of NO2- forme...
متن کاملIn vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase in Azotobacter vinelandii.
H2 oxidation in Azotobacter vinelandii is catalyzed by a membrane-bound, alpha beta dimeric [NiFe] hydrogenase. Maturation of the enzyme involves cleavage of a putative N-terminal signal sequence in the beta subunit and removal of 15 amino acids from the C terminus of the alpha subunit. Cells limited for nickel exhibited low hydrogenase activities and contained an apparently large form of the a...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1989
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.86.16.6082