Zobrazeno 1 - 10
of 131
pro vyhledávání: '"Takamitsu Kohzuma"'
Autor:
Takahide Yamaguchi, Kouhei Akao, Alexandros Koutsioubas, Henrich Frielinghaus, Takamitsu Kohzuma
Publikováno v:
Biomolecules, Vol 12, Iss 1, p 95 (2022)
The dynamic structure changes, including the unfolding, dimerization, and transition from the compact to the open-bundle unfolding intermediate structure of Cyt c′, were detected by a small-angle neutron scattering experiment (SANS). The structure
Externí odkaz:
https://doaj.org/article/ecd1cbb020d745798e9059913fc99226
Autor:
Yurie Edanami, Akira Yamaguchi, Takamitsu Kohzuma, Takahide Yamaguchi, Yuuta Shibuya, Norihisa Fukaya
Publikováno v:
Bulletin of the Chemical Society of Japan. 93:630-636
We studied copper coordination geometry in Type I copper protein pseudoazurin (PAz) within silica mesopores with a series of pore diameters. The adsorption of PAz into the silica mesopores was eval...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0945fb18e766bac77b5c4d8dd8193c12
https://doi.org/10.1246/bcsj.20190355
https://doi.org/10.1246/bcsj.20190355
Autor:
Takahide, Yamaguchi, Kouhei, Akao, Alexandros, Koutsioubas, Henrich, Frielinghaus, Takamitsu, Kohzuma
Publikováno v:
Biomolecules
The dynamic structure changes, including the unfolding, dimerization, and transition from the compact to the open-bundle unfolding intermediate structure of Cyt c′, were detected by a small-angle neutron scattering experiment (SANS). The structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7dbb7081a8a41af1d41d75356d89c2a5
https://pubmed.ncbi.nlm.nih.gov/35053243
https://pubmed.ncbi.nlm.nih.gov/35053243
Publikováno v:
Chemistry Letters. 49:1456-1458
The protein stability of the Met16Leu pseudoazurin (PAz) variant was examined by electrospray ionization mass spectrometry (ESI-MS), and the protein stability was similar to that of WT, which has a...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c6a96c6471f75732ddeb348bdc4ab90
https://doi.org/10.1246/cl.200578
https://doi.org/10.1246/cl.200578
Publikováno v:
Bulletin of the Chemical Society of Japan. 92:1874-1882
In view of the key roles played by noncovalent or weak interactions in biological processes, it is important to understand them at the molecular level. Based on the results of the thermodynamic, sp...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e4ff0a441dc023657c3b944a0f8dd47
https://doi.org/10.1246/bcsj.20190197
https://doi.org/10.1246/bcsj.20190197
Autor:
Takamitsu Kohzuma, Akira Shinoda, Fumiaki Yumoto, Toshiya Senda, Kotaro Koiwai, Takahide Yamaguchi, Yusuke Yamada, Naruhiko Adachi, Toshio Moriya, Masato Kawasaki
Cu-containing nitrite reductases (NiRs), a well-studied family of 110 kDa enzymes, play central roles in denitrification and have over 100 Protein Data Bank entries. However, such issues as crystal packing, photoreduction, and lack of high pH cases h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b13ff29404db98fcfe66d2bb0fd106b
https://doi.org/10.1101/2020.07.12.199695
https://doi.org/10.1101/2020.07.12.199695
Autor:
Fumiaki Yumoto, Akira Shinoda, Naruhiko Adachi, Takamitsu Kohzuma, Toshiya Senda, Takahide Yamaguchi, Toshio Moriya, Kotaro Koiwai, Yusuke Yamada, Masato Kawasaki
Publikováno v:
Journal of Structural Biology. 213:107768
Cu-containing nitrite reductases (NiRs) are 110 kDa enzymes that play central roles in denitrification. Although the NiRs have been well studied, with over 100 Protein Data Bank entries, such issues as crystal packing, photoreduction, and lack of hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7682dd08f2b642db41e0f3968136f150
https://doi.org/10.1016/j.jsb.2021.107768
https://doi.org/10.1016/j.jsb.2021.107768
Autor:
Yuko Nihei, Duncan E. K. Sutherland, Martin J. Stillman, Takahide Yamaguchi, Takamitsu Kohzuma
Publikováno v:
Protein Science. 26:1921-1931
Noncovalent, weak interactions in the second coordination sphere of the copper active site of Pseudoazurin (PAz) from Achromobacter cycloclastes were examined using a series of Met16X variants. In this study, the differences in protein stability due
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eadbfa0f820af12bddf79f43ef45fc49
https://doi.org/10.1002/pro.3226
https://doi.org/10.1002/pro.3226
Autor:
Masaki Unno, Takamitsu Kohzuma, Martin J. Stillman, Michael T. Tiedemann, Takahide Yamaguchi, Akiko Takashina
Publikováno v:
Bulletin of the Chemical Society of Japan. 90:169-177
The unusual magnetic/spectroscopic properties of Cytochrome c′ (Cyt c′) have been discussed, especially concerning the possibility of a quantum mechanically mixed-spin configuration of heme Fe(III). Here, four unique-spin species were identified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa74aff054608d0a3141420bb4dbeb22
https://doi.org/10.1246/bcsj.20160316
https://doi.org/10.1246/bcsj.20160316