Comparison of the purification and properties of MO-, V-, and Fe-nitrogenase from Azotobacter vinelandii
β Scribed by BrianJ. Hales; KathleenA. Scorsone; Virginia Moore
- Book ID
- 107901135
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 88 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0162-0134
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Nitrogenase of Azotobacter vindandii is sensitive to oxygen, and sensitivity develops during purification. Such inactivation is well prevented by 0.1% hydroquinone plus 0.01 ~ ascorbate, which are also effective in preventing inactivation of enzyme on storage under H2. Activity is proportional to fe
A sequence homologous to the conventional nifH gene has been cloned from a different region of the Azotobacter vinelandii genome. Tn5 insertions were obtained in this clone and the mutagenized plasmid was used for marker exchange with A. vinelandii strain CA12 (delta nifHDK) to obtain Tn5 mutants. T