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Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl‐Radical Transfer in the Coenzyme B 12 Dependent Enzyme Glutamate Mutase
Author(s) -
Gruber Karl,
Reitzer Riikka,
Kratky Christoph
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010917)40:18<3377::aid-anie3377>3.0.co;2-8
Subject(s) - pseudorotation , cofactor , chemistry , mutase , ribose , active site , enzyme , stereochemistry , substrate (aquarium) , ligand (biochemistry) , biochemistry , biology , organic chemistry , molecule , receptor , ecology
Two alternate conformations of the adenosyl ligand of the cofactor are observed in the active site of the coenzyme B 12 dependent enzyme glutamate mutase. This result shows ribose pseudorotation to be an elegant and safe mechanism for shuttling the “hot” methylene radical between the cofactor and substrate (see scheme).