T
Takashi Matsuo
Researcher at Nara Institute of Science and Technology
Publications - 59
Citations - 1603
Takashi Matsuo is an academic researcher from Nara Institute of Science and Technology. The author has contributed to research in topics: Myoglobin & Heme. The author has an hindex of 24, co-authored 59 publications receiving 1463 citations. Previous affiliations of Takashi Matsuo include National Archives and Records Administration & National Presto Industries.
Papers
More filters
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
Supramolecular Hemoprotein Linear Assembly by Successive Interprotein Heme−Heme Pocket Interactions
Hiroaki Kitagishi,Koji Oohora,Hiroyasu Yamaguchi,Hideaki Sato,Takashi Matsuo,and Akira Harada,Takashi Hayashi +6 more
TL;DR: The interprotein heme−heme pocket interaction produces a unique submicrometer-sized linear hemoprotein fiber, determined by size exclusion chromatography and atomic force microscopy.
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
Iron Porphyrin−Cyclodextrin Supramolecular Complex as a Functional Model of Myoglobin in Aqueous Solution
Koji Kano,Hiroaki Kitagishi,Camille Dagallier,Masahito Kodera,Takashi Matsuo,Takashi Hayashi,Yoshio Hisaeda,Shun Hirota +7 more
TL;DR: The 1:1 inclusion complex of 5,10,15,20-tetrakis(4-sulfonatophenyl)porphinato iron( II) (Fe(II)TPPS) and an O-methylated beta-cyclodextrin dimer having a pyridine linker binds dioxygen reversibly in aqueous solution.