The crystal structure of glutamate mutase with bound coenzyme B(12) suggests a radical shuttling mechanism within the active site of the enzyme. Quantum chemical calculations of the rearrangement in combination with kinetic and mutational studies suggest the catalytic mechanism of this enzyme to pro
โฆ LIBER โฆ
A biradical in coenzyme B12-dependent glutamate mutase during catalysis
โ Scribed by O. Zelder; B. Beatrix; W. Buckel
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 79 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0162-0134
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