𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Electron microscopy of the nitrogenase molecule from azotobacter vinelandii

✍ Scribed by V.L. Tsuprun; E.V. Orlova; N.A. Kiselev; I.Z. Mitsova; I.S. Blazshchuk; R.I. Gvozdev

Book ID
103567397
Publisher
Elsevier Science
Year
1986
Tongue
English
Weight
475 KB
Volume
27
Category
Article
ISSN
0162-0134

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Studies on the hydrogenation steps of th
Studies on the hydrogenation steps of the nitrogen molecule at the Azotobacter vinelandii nitrogenase site
✍ Krassimir K. Stavrev; Michael C. Zerner πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 479 KB πŸ‘ 2 views

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

Stability and ferrous iron content of th
Stability and ferrous iron content of the nitrogenase and its components from Azotobacter vinelandii
✍ Kajiyama, Shozo ;Nosoh, Yoshiaki πŸ“‚ Article πŸ“… 1972 πŸ› Springer-Verlag βš– 688 KB

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