Characterization of an oxygen-stable nitrogenase complex isolated from Azotobacter chroococcum
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چکیده
منابع مشابه
Characterization of an oxygen-stable nitrogenase complex isolated from Azotobacter chroococcum.
In crude cell-free extracts of Azotobacter chroococcum, nitrogenase was much less sensitive to irreversible inactivation by O2 than was the purified enzyme. When nitrogenase was partially purified by anaerobic discontinuous sucrose-density-gradient centrifugation, O2-tolerance was retained. This preparation was considerably enriched in four polypeptides, three of which were derived from the Mo-...
متن کاملNitrogenase 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
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...
متن کاملNature of oxygen inhibition of nitrogenase from Azotobacter vinelandii.
The reduction of nitrogen, acetylene, azide, and cyanide at various oxygen concentrations by nitrogenase from Azotobacter vinelandii was measured with a well-defined system. Oxygen inhibited the reduction of each substrate uncompetitively. The inhibition constants (K(i)) were 0.014, 0.023, 0.008, and 0.003 atm of oxygen for reduction of nitrogen, acetylene, azide, and cyanide, respectively. The...
متن کاملHydrazine is a product of dinitrogen reduction by the vanadium-nitrogenase from Azotobacter chroococcum.
During the enzymic reduction of N2 to NH3 by Mo-nitrogenase, free hydrazine (N2H4) is not detectable, but an enzyme-bound intermediate can be made to yield N2H4 by quenching the enzyme during turnover [Thorneley, Eady & Lowe (1978) Nature (London) 272, 557-558]. In contrast, we show here that the V-nitrogenase of Azotobacter chroococcum produces a small but significant amount of free N2H4 (up t...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1979
ISSN: 0264-6021
DOI: 10.1042/bj1810569