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Physical and chemical properties of the nitrogenase proteins fromAzotobacter vinelandii

✍ Scribed by D. Kleiner; C. H. Chen

Publisher: Springer
Year: 1974
Tongue: English
Weight: 570 KB
Volume: 98
Category: Article
ISSN: 0302-8933
DOI: 10.1007/bf00425272

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✦ Synopsis

The purified Mo-Fe protein and Fe protein of nitrogenase from Azotobacter vinelandii have molecular weights (MW) of about 216000 and 64000, respectively. The Mo-Fe protein is composed of subunits of about 56000 MW, and the Fe protein has 2 equivalent subunits of about 33000 MW. The isoelectric point of the Mo-Fe protein is 5.2 and that of the :Fe protein is 4.7. Amino acid compositions reflect the acidic nature of the proteins. The Mo-Fe protein yielded 24 atoms of Fe, 20 atoms of acid-labile sulfide and 1.54 atoms of Mo per molecule. Analysis of the Fe protein showed 3.45 atoms of Fe per molecule.

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