Stability and ferrous iron content of the nitrogenase and its components from Azotobacter vinelandii

✍ Scribed by Kajiyama, Shozo ;Nosoh, Yoshiaki

• Publisher: Springer-Verlag
• Year: 1972
• Weight: 688 KB
• Volume: 85
• Category: Article
• ISSN: 0003-9276
• DOI: 10.1007/bf00408843

✦ Synopsis

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 ferrous iron content of crude sample of enzyme. On storage at 0~ 0.3 M KC1 inactivates the enzyme, while KC1 stabilizes its components. Nitrogenase is not cold labile, while the components are cold labile; Fe, Mo-component is most stable at 22~ and Fe-component at 13.5~ Nitrogenase substrates, except N2, stabilize nitrogenase, but not the components.