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Nitrogenase from the photosynthetic bacterium Rhodopseudomonas capsulata: purification and molecular properties

Journal Article · · J. Bacteriol.; (United States)
OSTI ID:5103192
Nitrogenase proteins were isolated from cultures of the photosynthetic bacterium Rhodopseudomonas capsulata grown on a limiting amount of ammonia. Under these conditions, the nitrogenase N/sub 2/ase A was active in vivo, and nitrogenase activity in vitro was not dependent upon manganese and the activating factor. The nitrogenase proteins were also isolated from nitrogen-limited cultures in which the in vivo nitrogenase activity had been stopped by an ammonia shock. This nitrogenase activity, N/sub 2/ase R, showed an in vitro requirement for manganese and the activating factor for maximal activity. The Mo-Fe protein (dinitrogenase) was composed of two dissimilar subunits with molecular weights of 55,000 and 59,500; the Fe protein (dinitrogenase reductase), from either type of culture, was composed of a single subunit (molecular weight, 33,500). The metal and acid labile sulfur contents of both nitrogenase proteins were similar to those found for previously isolated nitrogenases. The Fe proteins from both N/sub 2/ase a and N/sub 2/ase R contained phosphate and ribose, 2 mol of each per mol of N/sub 2/ase R Fe protein contained about 1 mol per mol of an adenine-like molecule, whereas the N/sub 2/ase A Fe protein content of this compound was insignificant. These results are compared with various models previously presented for the short-term regulation of nitrogenase activity in the photosynthetic bacteria.
Research Organization:
Centre d'Etudes Nucleaires, Grenoble, France
OSTI ID:
5103192
Journal Information:
J. Bacteriol.; (United States), Journal Name: J. Bacteriol.; (United States) Vol. 149:2; ISSN JOBAA
Country of Publication:
United States
Language:
English