Compilation of heme oxygenase catalysis
Project/Area Number |
24350081
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Chemistry related to living body
|
Research Institution | Tohoku University |
Principal Investigator |
|
Co-Investigator(Renkei-kenkyūsha) |
TOSHITAKA Matsui 東北大学, 多元物質科学研究所, 准教授 (90323120)
MASAKI Unno 茨城大学, 理工学研究科, 教授 (10359549)
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥18,330,000 (Direct Cost: ¥14,100,000、Indirect Cost: ¥4,230,000)
Fiscal Year 2014: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2013: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2012: ¥6,500,000 (Direct Cost: ¥5,000,000、Indirect Cost: ¥1,500,000)
|
Keywords | ヘム / 酸素活性化 / 結晶構造解析 / 反応機構 / 共鳴ラマン散乱 / EPR / 分子動力学 / ヘム分解 / 結核菌 / 水酸化ヘム / ヘムオキシゲナーゼ / ヘム分解酵素 / ベルドヘム / 黄色ブドウ球菌 |
Outline of Final Research Achievements |
Heme oxygenase (HO) converts heme into biliverdin, CO, and iron by three step monooxygenation reactions. Crystal structures of the heme-free, iron-biliverdin and biliverdin complexes have been solved, and the HO protein structural changes associated with the heme-binding and biliverdin-release have been determined by the molecular dynamic simulations. In addition, the final reaction products of a new type heme degradation enzyme, MhuD of M. tuberculosis and its homologue IsdG of S. aureus, have been established. We have found that that these enzyme degrade heme without CO release, demonstrating a new way to degrade heme.
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Report
(4 results)
Research Products
(19 results)