Studies on archaeal antioxidation system involving thioredoxin proteins

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In order to elucidate the evolution process of antioxidation system in life from the viewpoint of protein science, we structurally characterized archaeal peroxiredoxin(Prx) and related antioxidant proteins. Especially, structure determination of the complex of Prx and its substrate, hydrogen peroxide, enabled discussion on the very early stage and the transition state of the Prx reaction. Furthermore, we determined the 3D structure of an archaeal cambialistic superoxide dismutase, which revealed the relationship between metal selectivity and the local 3D structure of the enzyme. Elucidation of protein reaction mechanism involving hydrogen atoms needs collection of neutron diffraction data of the protein. We developed methods for obtaining large protein crystals for the purpose of the neutron diffraction study.