On the reduced and oxidized forms of the FeMo- cofactor of Azotobacter vinelandii nitrogenase
β Scribed by Krassimir K. Stavrev; Michael C. Zerner
- Book ID
- 105886994
- Publisher
- Springer
- Year
- 1997
- Tongue
- English
- Weight
- 390 KB
- Volume
- 96
- Category
- Article
- ISSN
- 1432-2234
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π SIMILAR VOLUMES
We follow the initial activation of the nitrogen molecule at the FeMo cofactor of nitrogenase and subsequently model the hydrogenation of N up to the fourth 2 protonation step using the intermediate neglect of differential overlap quantum-chemical model. The results obtained favor a reaction mechani
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