2011 Fiscal Year Final Research Report
Reaction Mechanism of Heme Oxygenase
| Project/Area Number |
21350087
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
MATSUI Toshitaka 東北大学, 多元物質科学研究所, 講師 (90323120)
UNO Masaki 茨城大学, フロンティア応用原子科学研究センター, 准教授 (10359549)
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| Project Period (FY) |
2009 – 2011
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| Keywords | ヘム / 酸素活性化 / 結晶構造解析 / ベルドヘム / 反応機構 / 構造活性相関 |
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| Research Abstract |
Enzymatic heme degaradation by heme oxygenase, especially its rate-limiting ring opening step, have been studied in detail. Spectroscopic analysis reveals the formation of a ferryl species as a ring opening intermediate. Crystallographic study on an intermediate-enzyme complex combined with theoritical calculations finally elucidate the rate-limiting reaction. We also examined a novel heme cleavage reaction to clarify its mechanism and the new heme catabolites were succesufully detected from cultured mammalian cells.
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[Journal Article] Heme regulates B-cell differentiation, antibody class switch, and heme oxygenase-1 expression in B cell as a ligand of Bach22011
Author(s)
M. Watanabe-Matsui, A. Muto, T. Matsui, A. Itoh-Nakadai, O. Nakajima, K. Murayama, M. Yamamoto, M. Ikeda-Saito, K. Igarashi
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Journal Title
Blood
Volume: 117
Pages: 5438-5448
Peer Reviewed
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