H
Hiroyasu Tabe
Researcher at Osaka City University
Publications - 28
Citations - 389
Hiroyasu Tabe is an academic researcher from Osaka City University. The author has contributed to research in topics: Catalysis & Chemistry. The author has an hindex of 9, co-authored 20 publications receiving 289 citations. Previous affiliations of Hiroyasu Tabe include Kyoto University.
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Journal ArticleDOI
Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold
Hiroyasu Tabe,Kenta Fujita,Satoshi Abe,Masahiko Tsujimoto,Takahiro Kuchimaru,Shinae Kizaka-Kondoh,Mikio Takano,Susumu Kitagawa,Takafumi Ueno,Takafumi Ueno +9 more
TL;DR: The preparation of ruthenium carbonyl-incorporated cross-linked hen egg white lysozyme crystals (Ru·CL-HEWL) shows potential for use as an artificial extracellular scaffold suitable for transport and release of a gas molecule.
Journal ArticleDOI
Crystal Engineering of Self-Assembled Porous Protein Materials in Living Cells
Satoshi Abe,Hiroyasu Tabe,Hiroshi Ijiri,Keitaro Yamashita,Kunio Hirata,Kohei Atsumi,Takuya Shimoi,Masaki Akai,Hajime Mori,Susumu Kitagawa,Takafumi Ueno +10 more
TL;DR: It is reported that polyhedra, a natural crystalline protein assembly of polyhedrin monomer produced in insect cells infected by cypovirus, can be engineered to extend porous networks by deleting selected amino acid residues located on the intermolecular contact region of PhM.
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Post‐Crystal Engineering of Zinc‐Substituted Myoglobin to Construct a Long‐Lived Photoinduced Charge‐Separation System
Tomomi Koshiyama,Masanobu Shirai,Tatsuo Hikage,Hiroyasu Tabe,Koichiro Tanaka,Susumu Kitagawa,Takafumi Ueno,Takafumi Ueno +7 more
TL;DR: An artificial long-lived photoinduced charge-separation system using a protein crystal with different redox cofactors fixed in defined locations is constructed and the results suggest that these features are governed by steric repulsion and electrostatic interaction induced by amino acid residues located on the internal surface of the crystal lattices.
Journal ArticleDOI
Porous Protein Crystals as Catalytic Vessels for Organometallic Complexes
TL;DR: Ruthenium complexes in cross-linked porous hen egg white lysozyme crystals catalyzed the enantioselective hydrogen-transfer reduction of acetophenone derivatives and gave different enantiomers based on the crystal form (tetragonal or orthorhombic).
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Artificial metalloenzymes constructed from hierarchically-assembled proteins.
TL;DR: The development of artificial metalloenzymes with hierarchically-assembled proteins would enable us to provide powerful tools for industrial and biological applications.