How the Co−C Bond Is Cleaved in Coenzyme B12 Enzymes: A Theoretical Study
Author:
Affiliation:
1. Contribution from the Department of Theoretical Chemistry, Lund University, Chemical Center, P.O. Box 124, S-221 00 Lund, Sweden
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja050744i
Reference94 articles.
1. A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase
2. How a Protein Binds B 12 : A 3.0 Å X-Ray Structure of B 12 -Binding Domains of Methionine Synthase
3. How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution
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