Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Chizu Shimokawa"'
Autor:
Chizu Shimokawa, Nobutaka Fujieda, Shinobu Itoh, Haruyasu Asahara, Yuma Morimoto, June Takaichi, Takayuki Hojo, Nagatoshi Nishiwaki, Shunichi Fukuzumi, Hideki Sugimoto, Seiji Mori, Kei Ohkubo
Publikováno v:
Inorganic Chemistry. 53:6159-6169
Nickel complexes of a series of β-diketiminate ligands ((R)L(-), deprotonated form of 2-substituted N-[3-(phenylamino)allylidene]aniline derivatives (R)LH, R = Me, H, Br, CN, and NO2) have been synthesized and structurally characterized. One-electro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0adfd36ebd88c077f66dc262da83a466
https://doi.org/10.1021/ic5006693
https://doi.org/10.1021/ic5006693
Autor:
Michiaki Murata, Shinobu Itoh, Yukihiro Nakamura, Nobutaka Fujieda, Chizu Shimokawa, Shintaro Yabuta, Yoji Hata, Takuya Ikeda
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 18:19-26
The pro form of recombinant tyrosinase from Aspergillus oryzae (melB) shows no catalytic activity, but acid treatment (around pH 3.5) of protyrosinase activates it to induce tyrosinase activity. Circular dichroism spectra, gel filtration analysis, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6bdd4e5b2f6833abdd999aaabee44b7
https://doi.org/10.1007/s00775-012-0945-5
https://doi.org/10.1007/s00775-012-0945-5
Autor:
Nobutaka Fujieda, Shinobu Itoh, Yukihiro Nakamura, Shintaro Yabuta, Yoji Hata, Takuya Ikeda, Michiaki Murata, Chizu Shimokawa
Publikováno v:
ChemBioChem. 13:193-201
The pro form of melB tyrosinase from the melB gene of Aspergillus oryzae was over-produced from E. coli and formed a homodimer that exhibited the spectral features of met-tyrosinase. In the presence of NH(2)OH (reductant), the proenzyme bound dioxyge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b37e0ff73c77fc14a6723d55e5f62c9
https://doi.org/10.1002/cbic.201100609
https://doi.org/10.1002/cbic.201100609
Autor:
Jiro Harada, Masakazu Sugishima, Graham Palmer, Masato Noguchi, Hiroshi Sakamoto, Hideaki Sato, Yuichiro Higashimoto, Chizu Shimokawa
Publikováno v:
Journal of Inorganic Biochemistry. 105:289-296
Heme oxygenase (HO) catalyses the degradation of heme to biliverdin, carbon monoxide (CO) and ferrous iron via three successive monooxygenase reactions, using electrons provided by NADPH-cytochrome P450 reductase (CPR) and oxygen molecules. For cleav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ba29891d2ba5f7c7b719d16800089db
https://doi.org/10.1016/j.jinorgbio.2010.11.010
https://doi.org/10.1016/j.jinorgbio.2010.11.010
Publikováno v:
Bulletin of the Chemical Society of Japan. 83:1162-1169
Resonance Raman spectra are measured for copper(II) complexes ([Cu(RL)2]) using a series of β-diketiminate ligands (L) carrying different α-substituents (R = Me, H, CN, and NO2), and quantum chemic...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06554d43902d28680d92205ec8c8a97f
https://doi.org/10.1246/bcsj.20100124
https://doi.org/10.1246/bcsj.20100124
Publikováno v:
Journal of Inorganic Biochemistry. 100:1118-1127
The reaction of copper(II) complexes supported by a series of beta-diketiminate ligands ((R1,R2)L, [(Dipp)N-C(R(2))-C(R(1))-C(R(2))-N(Dipp)](-), Dipp=2,6-diisopropylphenyl; see ) and H(2)O(2) has been examined spectroscopically at a low temperature.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31a05bcff84dafe0d444b3b967ee3b0e
https://doi.org/10.1016/j.jinorgbio.2006.02.005
https://doi.org/10.1016/j.jinorgbio.2006.02.005
Publikováno v:
Bulletin of the Chemical Society of Japan. 79:118-125
Copper(I) complexes generated by using a series of β-diketiminate ligands (R1,R2LR3−, [(R3)N–C(R2)–C(R1)–C(R2)–N(R3)]−, see Chart 1; “β-diketiminate” denotes enaminone imine analogs) have been stru...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b610a5d259e94f96c3b1734dd4c86f6
https://doi.org/10.1246/bcsj.79.118
https://doi.org/10.1246/bcsj.79.118
Autor:
Shinobu Itoh, Chizu Shimokawa
Publikováno v:
Inorganic Chemistry. 44:3010-3012
Reactions of Ag(I) and a series of beta-diketiminate ligands have been investigated to demonstrate that unique macrocyclic dinuclear and tetranuclear Ag(I)-complexes and a linear coordination polymer Ag(I)-complex as well as oxidative C-C coupling di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03e8fef6a09a749311e5e9c423358013
https://doi.org/10.1021/ic0501014
https://doi.org/10.1021/ic0501014
Autor:
Masakazu Sugishima, Hideaki Sato, Saori Harada, Kenichi Takahashi, Chizu Shimokawa, Masato Noguchi, Yasuhiko Kaida, Yuichiro Higashimoto
Publikováno v:
Biochemistry. 48(7)
The peptide C-terminal amide group essential for the full biological activity of many peptide hormones is produced by consecutive actions of peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidylamidoglycolate lyase (PAL); PHM catalyzes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2d1fc7d181ef17f3e979d8e8d569b2f
https://pubmed.ncbi.nlm.nih.gov/19170548
https://pubmed.ncbi.nlm.nih.gov/19170548
Autor:
Masakazu Sugishima, Yuichiro Higashimoto, Graham Palmer, Hiroshi Sakamoto, Hideaki Sato, Keiichi Fukuyama, Chizu Shimokawa, Masato Noguchi
Publikováno v:
The Biochemical journal. 419(2)
HO (haem oxygenase) catalyses the degradation of haem to biliverdin, CO and ferrous iron via three successive oxygenation reactions, i.e. haem to alpha-hydroxyhaem, alpha-hydroxyhaem to alpha-verdohaem and alpha-verdohaem to ferric biliverdin-iron ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e4ec1a19cd1b3fd1516d6260e977440
https://pubmed.ncbi.nlm.nih.gov/19154182
https://pubmed.ncbi.nlm.nih.gov/19154182