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

4. Elucidation of structure-function relationship of cytochrome c

Thermophile Hydrogenobacter thermophilus cytochrome c552 (HT) and mesophile Pseudomonas aeruginosa cytochrome c551 (PA) are small monoheme-containing electron transfer proteins composed of 80 and 82 amino acid residues, respectively. The two proteins exhibit high sequence identity (56 %), and their main-chain folding is almost identical. Despite their structural similarity, there is remarkable disparity in their thermostability and redox properties; the denaturation temperatures of PA in both the reduced and oxidized forms are considerably lower than those of HT in the corresponding forms, and the redox potential of PA at pH 6.0 and 25 °C is higher by ~60 mV relative to that of HT. We are elucidating structure-function relationship of cytochrome c through a detailed comparison between structural and functional properties of HT and PA.

Steric structures of Hydrogenobacter thermophilus cytochrome c552 (HT) and Pseudomonas aeruginosa cytochrome c551 (PA)

 

Plots of the standard redox potetials (Eo') against pH for wild-type PA and mutants.

 

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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