2013 Fiscal Year Final Research Report
Paradigm shift in enzymatic heme degradation
| Project/Area Number |
23550186
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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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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| Project Period (FY) |
2011 – 2013
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| Keywords | ヘム代謝 / 酸素活性化 / 反応機構 / 病原性細菌 / ホルムアルデヒド |
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| Research Abstract |
In this study, we have examined novel type reactions of enzymatic heme degradation. A recent in vitro study has revealed that a canonical heme degrading enzyme, heme oxygenase (HO), produces a new heme catabolite under special reaction condition. The new catabolite was successfully detected from mammalian cell culture, suggesting that the novel HO reaction can proceed in living organisms. On the other hand, newly-found IsdG-type enzymes degraded heme into unique reaction products through distinct reaction mechanisms. The mechanistic difference from the well-studied HO reaction appears to be caused by unusual non-planarity of heme bound to the IsdG-type enzymes. These diversity shed new light on enzymatic heme degradation to stimulate biological research exploring new physiological functions as well as its mechanistic studies.
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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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