3-D Geometry of Reactant Centers in the Co(II)-Substrate Radical Pair State of the B12 Enzyme, Ethanolamine Deaminase

Structure determinations at sub-bond length (<Å) spatial resolution are essential for the detailed description of molecular mechanism.

We have determined the 3-dimensional geometry of reactant centers in the active site of the Co(II)-substrate radical pair state of ethanolamine deaminase from Salmonella typhimurium. The Co(II)-substrate radical pair is a key intermediate in enzyme catalysis.

The following provides a brief synopsis of this work and the principal conclusions.

For a more detailed account, please see: Canfield, J. M. and Warncke, K. J. Phys. Chem. B. 2002, 106, 8831-8841.