Skip to main content
Article thumbnail
Location of Repository

Magnetic Field Effect Studies Indicate Reduced Geminate Recombination of the Radical Pair in Substrate Bound Adenosylcobalamin-Dependent Ethanolamine Ammonia Lyase

By Alex R. Jones, Sam Hay, Jonathan R. Woodward and Nigel S. Scrutton


Full-text of this article is not available on the LRA. The published version is available at:\ud DOI: 10.1021/ja077124xThe apparent conflict between literature evidence for (i) radical pair (RP) stabilization in adenosylcobalamin (AdoCbl)-dependent enzymes and (ii) the manifestation of magnetic field sensitivity due to appreciable geminate recombination of the RP has been reconciled by pre-steady-state magnetic field effect (MFE) investigations with ethanolamine ammonia lyase (EAL). We have shown previous stopped-flow MFE studies to be insensitive to magnetically induced changes in the net forward rate of C−Co homolytic bond cleavage. Subsequently, we observed a magnetic-dependence in the continuous-wave C−Co photolysis of free AdoCbl in 75% glycerol but have not done so in the thermal homolysis of this bond in the enzyme-bound cofactor in the presence of substrate. Consequently, in the enzyme-bound state, the RP generated upon homolysis appears to be stabilized against the extent of geminate recombination required to observe an MFE. These findings have strong implications for the mechanism of RP stabilization and the unprecedented catalytic power of this important class of cobalamin-dependent enzymes

Publisher: American Chemical Society publications
Year: 2007
DOI identifier: 10.1021/ja077124x
OAI identifier:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • (external link)
  • (external link)
  • (external link)
  • (external link)
  • Suggested articles

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.