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eLearning

SINAPSE experts from around Scotland have developed ten online modules designed to explain medical imaging. They are freely available and are intended for non-specialists.


Edinburgh Imaging Academy at the University of Edinburgh offers the following online programmes through a virtual learning environment:

Neuroimaging for Research MSc/Dip/Cert

Imaging MSc/Dip/Cert

PET-MR Principles & Applications Cert

Applied Medical Image Analysis Cert

Online Short Courses

Assay for the enantiomeric analysis of [H-2(1)]-fluoroacetic acid: Insight into the stereochemical course of fluorination during fluorometabolite biosynthesis in Streptomyces cattleya

Author(s): D. O'Hagan, R. J. M. Goss, A. Meddour, J. Courtieu

Abstract:
A sensitive method for the configurational analysis of (R)- and (S)-[H-2(1)]-fluoroacetate has been developed using H-2{H-1}-NMR in a chiral liquid crystalline solvent. This has enabled biosynthetic experiments to be conducted which reveal stereochemical details on biological fluorination occurring during the biosynthesis of fluoroacetate and 4-fluorothreonine in the bacterium Streptomyces cattleya. In particular, feeding experiments to S. cattleya with isotopically labeled (1R, 2R)- and (1S, 2R)-[1-H-2(1)]-glycerol 3d and 3e and [2,3-H-2(4)]-Succinate 4a gave rise to samples of enantiomerically enriched [2-H-2(1)]-fluoroacetates 1a. The predominant enantiomer resulting from each experiment suggests that the stereochemical course of biological fluorination takes place with an overall retention of configuration between a glycolytic intermediate and fluoroacetate 1. Consequently, this outcome suggests that the stereochemical course of the recently identified fluorinase enzyme which mediates a reaction between fluoride ion and S-adenosyl-L-methionine (SAM), occurs with an inversion of configuration.

Full version: Available here

Click the link to go to an external website with the full version of the paper


ISBN: 0002-7863
Publication Year: 2003
Periodical: Journal of the American Chemical Society
Periodical Number: 2
Volume: 125
Pages: 379-387
Author Address: