Abstract

The mechanism of cyclization of uridine-3(-p-nitrophenyl phosphate catalyzed by various transition metals has been studied using heavy atom isotope effects. The positions where relevant isotope effects are measured are the nitro nitrogen and all phosphate oxygens. The isotope effect of the nitro nitrogen has been measured with several different transition metal catalysts and the data indicate significant delocalization of electrons into the ring in the transition state. The synthesis of compounds isotopically labeled at the phosphate oxygens is underway. These compounds will be used to determine the oxygen isotope effects, which will provide additional insight into the structure of the transition state of phosphate cyclization. This will allow the mechanism of these reactions to be better understood.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002301-12
Application #
5223893
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
12
Fiscal Year
1996
Total Cost
Indirect Cost

  Publications

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Assadi-Porter, Fariba M; Reiland, Hannah; Sabatini, Martina et al. (2018) Metabolic Reprogramming by 3-Iodothyronamine (T1AM): A New Perspective to Reverse Obesity through Co-Regulation of Sirtuin 4 and 6 Expression. Int J Mol Sci 19:
Dominguez, Eddie; Zarnowski, Robert; Sanchez, Hiram et al. (2018) Conservation and Divergence in the Candida Species Biofilm Matrix Mannan-Glucan Complex Structure, Function, and Genetic Control. MBio 9:
Franco, Aldo; Dovell, Sanaz; Möller, Carolina et al. (2018) Structural plasticity of mini-M conotoxins - expression of all mini-M subtypes by Conus regius. FEBS J 285:887-902
Selen Alpergin, Ebru S; Bolandnazar, Zeinab; Sabatini, Martina et al. (2017) Metabolic profiling reveals reprogramming of lipid metabolic pathways in treatment of polycystic ovary syndrome with 3-iodothyronamine. Physiol Rep 5:
Mong, Surin K; Cochran, Frank V; Yu, Hongtao et al. (2017) Heterochiral Knottin Protein: Folding and Solution Structure. Biochemistry 56:5720-5725

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