Electron Transport to Nitrogenase in Azotobacter chroococcum. Purification and Some Properties of NADH Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Nitrogenase in Azotobacter chroococcum and Klebsiella pneumoniae.
Blumberg, W. E. & Peisach, J. (1974) Arch. Biochem. Biophys. 162,502-512 Cammack, R. (1973) Biochem. Biophys. Res. Commun. 54,548-554 Cammack, R., Rao, K. K. & Hall, D. 0. (1971) Biochem. Biophys. Res. Commun. 44,s-14 Coffman, R. E. & Stavens, B. W. (1970) Biochem. Biophys. Res. Commun. 41,163-169 Fee, J. A. & Palmer, G. (1971) Biochim. Biophys. Actu 249,175-195 Genonde, Ic, Schlaak, M. E., Bri...
متن کاملThe vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the VFe protein.
1. Nitrogenase activity of a strain of Azotobacter chroococcum lacking the structural genes for conventional nitrogenase (nifHDK) was separated into two components: an Fe-containing protein and a vanadoprotein. 2. The larger protein was purified to homogeneity by the criterion of electrophoresis of 10% (w/v) acrylamide gels in the presence of SDS. Two types of subunit, of Mr 50,000 and 55,000, ...
متن کاملThe vanadium nitrogenase of Azotobacter chroococcum
1. Nitrogenase activity of a strain of Azotobacter chroococcum lacking the structural genes of Monitrogenase (nifHDK) was associated with a V+Fe-containing protein and an Fe-containing protein [Robson, Eady, Richardson, Miller, Hawkins & Postgate (1986) Nature (London) 322, 388-390; Eady, Robson, Richardson, Miller & Hawkins (1987) Biochem. J. 244, 197-207]. 2. The Fe protein was purifed to hom...
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in this thesis, at first we investigate the bounded inverse theorem on fuzzy normed linear spaces and study the set of all compact operators on these spaces. then we introduce the notions of fuzzy boundedness and investigate a new norm operators and the relationship between continuity and boundedness. and, we show that the space of all fuzzy bounded operators is complete. finally, we define...
15 صفحه اولMolybdenum nitrogenase of Azotobacter chroococcum. Tight binding of MgADP to the MoFe protein.
The dye-oxidized or dithionite-reduced forms of the MoFe protein of molybdenum nitrogenase of Azotobacter chroococcum were shown to bind 2 mol of MgADP/mol of protein, as determined by column equilibrium techniques. The gel-filtration elution profile of unbound Mg[14C]ADP was not symmetrical, consistent with a low rate of dissociation from the protein. Symmetrical elution profiles were observed...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1971
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1971.tb19693.x