D
Dai Murata
Researcher at Kyushu University
Publications - 4
Citations - 321
Dai Murata is an academic researcher from Kyushu University. The author has contributed to research in topics: Myoglobin & Heme. The author has an hindex of 4, co-authored 4 publications receiving 288 citations. Previous affiliations of Dai Murata include Kyoto Pharmaceutical University.
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Journal ArticleDOI
Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity
TL;DR: The present study indicates that the replacement of native heme with an artificially created prosthetic group will give us a unique function into a hemoprotein.
Journal ArticleDOI
Ligand binding properties of myoglobin reconstituted with iron porphycene: unusual O2 binding selectivity against CO binding.
Takashi Matsuo,Hirohisa Dejima,Shun Hirota,Dai Murata,Hideaki Sato,Takahiro Ikegami,Hiroshi Hori,Yoshio Hisaeda,Takashi Hayashi +8 more
TL;DR: The high O2 affinity and the unique characteristics of the myoglobin with the iron porphycene indicate that reconstitution with a synthesized heme is a useful method not only to understand the physiological function of myoglobin but also to create a tailor-made function on the protein.
Journal ArticleDOI
Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene.
Takashi Hayashi,Dai Murata,Masatomo Makino,Hiroshi Sugimoto,Takashi Matsuo,Hideaki Sato,Yoshitsugu Shiro,Yoshio Hisaeda +7 more
TL;DR: It was found that the reconstituted myoglobin catalyzed the H2O2-dependent oxidations of substrates such as guaiacol, thioanisole, and styrene, and it is a rare example that compound III is formed via compound II in myoglobin chemistry.
Journal ArticleDOI
Porphyrinoid chemistry in hemoprotein matrix: detection and reactivities of iron(IV)-oxo species of porphycene incorporated into horseradish peroxidase.
TL;DR: The kinetic analyses indicated that the ferric porphycene in the protein more slowly reacts with hydrogen peroxide than the native heme, whereas the high oxidation states show higher reactivities during oxidations of an organic substrate.