2010 Fiscal Year Final Research Report
Functional Modification of Oxygen Carrier Protein Hemocyanin and Its Application
Project/Area Number |
20350082
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Chemistry related to living body
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Research Institution | Osaka University |
Principal Investigator |
ITOH Shinobu Osaka University, 工学研究科, 教授 (30184659)
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Co-Investigator(Renkei-kenkyūsha) |
SUZUKI Shin-Ichiro 大阪大学, 理学研究科, 教授 (70116052)
AONO Shigetoshi 大学共同利用機関法人自然科学研究機構, 岡崎統合バイオサンエンスセンター, 教授 (60183729)
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Project Period (FY) |
2008 – 2010
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Keywords | 銅タンパク質 / ヘモシアニン / チロシナーゼ / 機能改変 / 分子状酸素の活性化 / フェノールの酸素化反応 / ペルオキソ二核銅酸素錯体 / 酸化反応機構 |
Research Abstract |
Hemocyanin functions as the oxygen carrier and storage protein in the hemolymph of many mollusks and arthropods. In this study, we have found that hemocyanin can also act as a monooxygenase enzyme when it is treated with denaturant such as urea. Spectroscopic features of the active oxygen species, (?-?^2:?^2-peroxo)dicopper(II), as well as the oxygenation mechanism of phenols have been explored in detail. Furthermore, catalytic oxygenation reaction of phenols by hemocyanin has been developed as an environmentally benign oxygenation process.
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[Journal Article] Post-translational His-Cys Cross Linkage Formation in Tyrosinase Induced by Copper(II)-Peroxo Species.2011
Author(s)
Nobutaka Fujieda, Takuya Ikeda, Michiaki Murata, Sachiko Yanagisawa, Shigetoshi Aono, Kei Ohkubo, Satoshi Nagao, Takashi Ogura, Shun Hirota, Shunichi Fukuzumi, Yukihiro Nakamura, Yoji Hata, Shinobu Itoh
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Journal Title
J.Am.Chem.Soc. 133(5)
Pages: 1180-1183
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