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Solid-state 2H NMR study of methyl-d3-cobalamin

J R Garbutt1, G R Goward, C W Kirby

  • 1Guelph-Waterloo Centre for Graduate Work in Chemistry and Biochemistry, Department of Chemistry, University of Waterloo, ON, Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|January 29, 1999
PubMed
Summary

Solid-state 2H NMR reveals methyl-d3-cobalamin

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Area of Science:

  • Bioorganometallic chemistry
  • Solid-state nuclear magnetic resonance (NMR) spectroscopy
  • Methyl-d3-cobalamin dynamics

Background:

  • Cobalamin is a crucial coenzyme in biological systems.
  • Understanding the dynamics of the methyl group in cobalamin is essential for elucidating its enzymatic mechanisms.
  • Methyl-d3-cobalamin serves as a model compound for studying these dynamics.

Purpose of the Study:

  • To investigate the motion and energetics of the methyl group in methyl-d3-cobalamin.
  • To determine the Co-C-2H bond angle.
  • To characterize the activation energy for methyl group motion.

Main Methods:

  • Solid-state 2H NMR spectroscopy was employed.
  • Temperature-dependent studies were conducted.
  • 2H NMR line shape analysis and spin-lattice relaxation time (T1) measurements were performed.

Main Results:

  • The methyl group exhibits rapid three-fold rotation.
  • The Co-C-2H angle was determined to be between 105.9 and 109.5 degrees.
  • Anisotropic relaxation indicates a
  • jumping
  • motion, with an activation energy of 8.3 ± 1.3 kJ/mol.

Conclusions:

  • The methyl group motion in methyl-d3-cobalamin is characterized by rapid rotation and anisotropic jumps.
  • The determined activation energy provides insight into the Co-C bond energetics.
  • This energetic barrier may serve as a probe for changes in the Co-C bond during enzymatic catalysis, such as in methionine synthase.

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