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Wiley, Angewandte Chemie International Edition, 18(40), p. 3377-3380, 2001

DOI: 10.1002/1521-3773(20010917)40:18<3377::aid-anie3377>3.0.co;2-8

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Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl‐Radical Transfer in the Coenzyme B12 Dependent Enzyme Glutamate Mutase

Journal article published in 2001 by Karl Gruber ORCID, Riikka Reitzer, Christoph Kratky
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Two alternate conformations of the adenosyl ligand of the cofactor are observed in the active site of the coenzyme B12 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).