Literature summary for 1.1.98.6 extracted from

Cho, K.; Himo, F.; Gr�slund, A.; Siegbahn, P.
The substrate reaction mechanism of class III anaerobic ribonucleotide reductase (2001), J. Phys. Chem. B, 105, 6445-6452.

No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment)	Organism
quantum chemical calculation of reaction mechanism. Carbon dioxide is formed from formate, which is present as a cofactor. The formate first forms a formyl radical. The next step, where the formyl radical protonates the 3'-keto group of the substrate, is rate limiting with a calculated total barrier of 19.9 kcal/mol, in reasonable agreement with the experimental rate-limiting barrier of 17 kcal/mol. Zero-point and entropy effects are quite significant in lowering the barrier	Escherichia coli

Crystallization (Comment)

Organism

quantum chemical calculation of reaction mechanism. Carbon dioxide is formed from formate, which is present as a cofactor. The formate first forms a formyl radical. The next step, where the formyl radical protonates the 3'-keto group of the substrate, is rate limiting with a calculated total barrier of 19.9 kcal/mol, in reasonable agreement with the experimental rate-limiting barrier of 17 kcal/mol. Zero-point and entropy effects are quite significant in lowering the barrier

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)