Research

  1. NMR of paramagnetic molecules
  2. Electronic manipulation of functional properties of myoglobin
  3. Structural and functional characterization of heme-DNA complexes
  4. Elucidation of structure-function relationship of cytochrome c
  5. Development of artificial blood-substitutes

1. NMR of paramagnetic molecules

The use of paramagnetic ions as extrinsic shift and relaxation probes for investigating the structure of biological molecules in solution has been exploited extensively. Taking advantage of the properties of unpaired electron(s) of a molecule, resonances arising from nuclei located in the close proximity of the paramagnetic center exhibit paramagnetic shifts and hence appear outside of the diamagnetic envelope, i.e., usual chemical shift range. Paramagnetically-shifted signals are extremely sensitive to structural and dynamic properties of molecules. We are applying various NMR methodologies to paramagnetic molecules possessing a wide range of shifts, line widths and relaxation times.

The 19F NMR spectra of myoglobin reconstituted with 2-MF heme. In response to a wide variety of electronic structure, 19F NMR signals are observed over a wide range of shifts, about 300 ppm.

 

The pH dependence of 19F NMR spectra in metmyoglobin reconstituted with 7-PF.

 

1H NMR spectra of the oxidized cytocrome c of the wild-type HT and mutants(left) and the coordination structure of heme in cytocrome c.

 

 

 

Menu

Home
research
publication
member
picture
Access
Link
japanese
    

Contact

1-1-1 Tennodai, Tsukuba Ibaraki 305-8571, Japan
Laboratory of Bioinorganic Chemistry,
Department of Chemistry,
Graduate School of Pure and Applied Sciences,Department of Chemistry, University of Tsukuba
Yasuhiko YAMAMOTO
Phone/Fax: +81-29-853-6521
Email:

2016.4.1 Update