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

2. Electronic manipulation of functional properties of myoglobin

Not only dioxygen (O2), but also as carbon monoxide (CO) is reversibly bound to a ferrous heme Fe atom (Fe(II)) in myoglobin (Mb). As an O2 storage protein, Mb must discriminate O2 against the toxic ligand CO ubiquitously produced from a variety of sources in biological systems. The ligand binding affinity of unencumbered model heme Fe(II) complexes is ~2×104 times higher for CO than for O2, but this ratio is considerably reduced in the proteins. In addition to distal histidine residue (His64), we found that the O2 affinity of Mb is largely affected by electron density of the heme Fe atom (ρFe), whereas the CO one is almost independent of the ρFe value. We are developing a technique which enables us to optimize functional properties of Mb as artificial blood-substitutes through electronic tuning of the intrinsic heme Fe reactivity.

Schematic representation of heme reconstitution of myoglobin.

 

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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