2013 Fiscal Year Final Research Report
Creation of Novel Functional Protein by Self-hydroxylation
| Project/Area Number |
24655153
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Chemistry related to living body
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| Research Institution | Osaka University |
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Principal Investigator |
FUJIEDA Nobutaka 大阪大学, 工学(系)研究科(研究院), 助教 (00452318)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | 非ヘム鉄酵素 / 酸化的自己修飾 / 翻訳後化学修飾 / ビルトイン補酵素 |
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| Research Abstract |
Recently, many self-hydroxylation reactions have reported, which occurred of aromatic amino acids lying close to mononuclear and dinuclear iron and copper binding site. In this study, we utilized cupin family protein bearing three or four histidine binding motif (3-His or 4-His motif) as metal binding scaffold. In the mutant introduced one tyrosine into the location of Ile49 or Trp56, non-natural occurring unusual spectral species around 800 nm have been found. Thus, the modification method presented in this study is very powerful to construct new functional protein for novel devices of bioelectronics and artificial metalloenzyme to be able to catalyze multielectron transfer reactions.
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[Journal Article] Activation Mechanism of MelB Tyrosinase from Aspergillus oryzae by acidic treatment2013
Author(s)
Fujieda, N., Murata, M., Yabuta, S., Ikeda, T., Shimokawa, C., Nakamura, Y., Hata, Y., and Itoh, S
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Journal Title
J. Biol. Inorg. Chem
Volume: 18
Pages: 19-26
Peer Reviewed
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[Journal Article] Crystal Structures of Copper-depleted and Copper-bound Fungal Pro-tyrosinase : Insights into Endogenous Cysteine-dependent Copper Incorporation2013
Author(s)
Fujieda, N., Yabuta, S., Ikeda, T., Oyama, T., Muraki, N., Kurisu, G., and Itoh, S
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Journal Title
J. Biol. Chem
Volume: 288
Pages: 22128-22140
Peer Reviewed
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