Structural genes for the vanadium nitrogenase from Azotobacter chroococcum.

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The 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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Hydrazine 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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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...

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The 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, ...

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Vanadium K-edge X-ray-absorption spectroscopy of the functioning and thionine-oxidized forms of the VFe-protein of the vanadium nitrogenase from Azotobacter chroococcum.

Vanadium K-edge X-ray-absorption spectra were collected for samples of thionine-oxidized, super-reduced (during enzyme turnover) and dithionite-reduced VFe-protein of the vanadium nitrogenase of Azotobacter chroococcum (Acl*). Both the e.x.a.f.s and the x.a.n.e.s. (X-ray-absorption near-edge structure) are consistent with the vanadium being present as part of a VFeS cluster; the environment of ...

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ژورنال

عنوان ژورنال: The EMBO Journal

سال: 1989

ISSN: 0261-4189

DOI: 10.1002/j.1460-2075.1989.tb03495.x