Výsledky vyhledávání - "Akimitsu Miyaji"

Akademický článek

Identifying the chloroperoxyl radical in acidified sodium chlorite solution.

Autor: Hiroyuki Kawata, Masahiro Kohno, Kohei Nukina, Isanori Horiuchi, Hisataka Goda, Tomomi Kuwahara, Kosei Yoshimori, Akimitsu Miyaji, Toshiaki Kamachi, Toshikazu Yoshikawa

Publikováno v: PLoS ONE, Vol 16, Iss 5, p e0252079 (2021)

The present study identified the active radical species in acidic sodium chlorite and investigated the feasibility of quantifying these species with the diethylphenylenediamine (DPD) method. Electron spin resonance (ESR) spectroscopy was used to iden

Externí odkaz: https://doaj.org/article/47960156cd564a6eab723cfec04dc789

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Mechanism of Formate Dehydrogenase Catalyzed CO2 Reduction with the Cation Radical of a 2,2′-Bipyridinium Salt Based on a Theoretical Approach

Autor: Akimitsu Miyaji, Yutaka Amao

The visible-light driven redox system of an electron donor, a photosensitizer, an electron mediator and formate dehydrogenase from Candida boidinii (CbFDH; EC.1.2.1.2) as a catalyst has received much attention for CO2 reduction to formate. In this sy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64b826890b3aafb9cde7a60d21d0412a
http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100886924

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Visible-light driven reduction of CO2 to formate by a water-soluble zinc porphyrin and formate dehydrogenase system with electron-mediated amino and carbamoyl group-modified viologen

Autor: Akimitsu Miyaji, Yutaka Amao

Publikováno v: New Journal of Chemistry. 45:5780-5790

Visible-light-driven CO2 reduction to formate with a system consisting of water-soluble zinc tetraphenylporphyrin tetrasulfonate (ZnTPPS), formate dehydrogenase from Candida boidinii (CbFDH) and 1-amino-1′-carbamoyl-4,4′-bipyridinium salt (ACBP)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4e6b6e0d94a5a5d4726356ee1cc50b3
https://doi.org/10.1039/d1nj00889g

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How does methylviologen cation radical supply two electrons to the formate dehydrogenase in the catalytic reduction process of CO2 to formate?

Autor: Yutaka Amao, Akimitsu Miyaji

Publikováno v: Physical Chemistry Chemical Physics. 22:18595-18605

Formate dehydrogenase from Candida boidinii (EC.1.2.1.2; CbFDH) is a commercially available enzyme and can be easily handled as a catalyst for the CO2 reduction to formate in the presence of NADH, single-electron reduced methylviologen (MV+˙) and so

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29f027ebf96cea3d09e40a761ebda4e7
https://doi.org/10.1039/d0cp02665d

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Theoretical study on CO2 reduction catalyzed by formate dehydrogenase using the cation radical of a bipyridinium salt with an ionic substituent as a co-enzym

Autor: Yutaka Amao, Akimitsu Miyaji

Publikováno v: Physical Chemistry Chemical Physics.

Formate dehydrogenase from Candida boidinii (CbFDH; EC.1.2.1.2) is a useful enzyme for CO2 reduction to formate in the photoredox system of a visible-light sensitizer and an electron mediator in the presence of an electron donor. The electron mediato

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88a518d2adca1a9804a7b9bebd2bd607
http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100835447

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How does methylviologen cation radical supply two electrons to the formate dehydrogenase in the catalytic reduction process of CO

Autor: Akimitsu, Miyaji, Yutaka, Amao

Publikováno v: Physical chemistry chemical physics : PCCP. 22(33)

Formate dehydrogenase from Candida boidinii (EC.1.2.1.2; CbFDH) is a commercially available enzyme and can be easily handled as a catalyst for the CO

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e287a809f8fad49f20a5438aa670e847
https://pubmed.ncbi.nlm.nih.gov/32785412

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Influence of tryptic hydrolysis on the enzymatic function of the membrane-bound form of particulate methane monooxygenase from Methylosinus trichosporium OB3b

Autor: Keita Satou, Toshihide Baba, Akimitsu Miyaji

Publikováno v: Journal of biotechnology. 323

Particulate methane monooxygenase (pMMO) is a membrane protein embedded in the intracytoplasmic membrane of methane-oxidizing bacteria. Structural analysis of pMMO showed the existence of a hydrophilic region exposed outside of the bacterial membrane

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e2d0586d48be61bde88bbc97810ef0c
https://pubmed.ncbi.nlm.nih.gov/32828830

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