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Articles by Tomoki Himiyama
A cytokine-based designer enzyme with an abiological multinuclear metal center exhibits intrinsic and extrinsic catalysis - Nature Communications
Abstract A designer enzyme consisting of an abiological molecule incorporated into a natural protein has been developed as an exceptionally chemoselective catalyst, highlighting that the internal space of proteins is highly beneficial for enhancing catalytic performance.
Cover Picture: Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity (Angew. Chem. Int. Ed. 36/2024)
Catalytic cyclopropanation reactions are demonstrated in the Research Article (e202403485) by Koji Oohora, Takashi Hayashi et al. using myoglobins reconstituted with artificial cofactors with various redox potentials. The cover image illustrates this catalysis by showing two types of protein-based trucks carrying rice ears (starting material) to produce rice sacks (product). The elevation profiles of the routes represent the differences in the reaction energy at the active center for each cofactor.
Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity
Introduction Heme, a porphyrin iron complex, is a ubiquitous cofactor which provides proteins with functions such as diatomic gas-binding, electron transfer, chemical catalysis, and transcriptional regulation among others. The unique reactivity of heme has been investigated in various heme-dependent enzymes.
Cooperative Catalysis of an Alcohol Dehydrogenase and Rhodium‐Modified Periodic Mesoporous Organosilica
Communication Cooperative Catalysis of an Alcohol Dehydrogenase and Rhodium‐Modified Periodic Mesoporous Organosilica Shinji Inagaki Corresponding Author E-mail address: inagaki@mosk.tytlabs.co.jp Toyota Central R&D Labs., Inc., Inagaki Senior Fellow Laboratory, Yokomichi, 480-1192 Nagakute, JAPAN Search for more papers by this author PDF PDF Share Abstract The combined use of a metal complex catalyst and an enzyme is an attractive concept, but typically results in mutual inactivation.
A Pyrene-Linked Cavity within a β-Barrel Protein Promotes an Asymmetric Diels-Alder Reaction
A pyrene-linked protein cavity attracts two substrate molecules like the scent of a flower attracts butterflies. In their Communication (DOI: 10.1002/anie.201704524), A. Onoda, T. Hayashi, and co-workers demonstrate that a polycyclic pyrene moiety linked within the rigid protein scaffold of the ?-barrel of nitrobindin acts as a platform to provide an aromatic interaction with a substrate.
A Pyrene-Linked Cavity within a β-Barrel Protein Promotes an Asymmetric Diels-Alder Reaction
A unique ?-expanded reaction cavity tethering a polycyclic moiety which provides a platform for substrate binding was constructed within the robust ?-barrel structure of nitrobindin (NB). NB variants with cavities of different sizes and shapes are coupled with N-(1-pyrenyl)maleimide (Pyr) to prepare a series of NB-Pyr conjugates. The orientation of the pyrene moiety is fixed within the cavity by the coupling reaction.
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