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[Heme (iron porphyrin complex)] Heme proteins are closely related to the oxygen metabolism in the living system, and thus play a crucial role in the maintenance of life. They commonly contain a heme cofactor, which is an iron porphyrin complex. Oxygen gas taken up by the respiration is delivered by hemoglobin to cells, where it is consumed by mitochondrial cytochrome oxidase in the electron transfer system. A part of oxygen is utilized by cytochromes P450 in the hormone synthesis and drug metabolism. Prostaglandin synthase, which is a key enzyme in the arachidonic cascade and is a target for aspirin and ibuprofen, soluble guanylate cyclase in the signal transmission system, and NO synthases are members of heme proteins, too.
As mentioned above, heme proteins are closely related to some of the drugs. In our Analytical Chemistry Group, we hope to contribute to the understanding of life and development of more efficient drugs, through studies on the structure-function relationships of heme proteins. We clone target genes with DNA recombination technique and construct over-expression systems. With highly purified proteins, we analyze their structure by way of molecular spectroscopy and measure biological activities. We prepare site-directed mutants of the protein and identify residues responsible for their structural specificities, activities, and drug binding. [DNA recombination]
In summary, our group of Analytical Chemistry hopes to contribute to the development of novel drugs through the studies on the structure and function of heme proteins closely related to oxygen metabolism.

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