Fine structures of reaction inter-mediates of bovine cytochrome c oxidase
Project/Area Number |
18K06092
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Review Section |
Basic Section 43020:Structural biochemistry-related
|
Research Institution | University of Hyogo |
Principal Investigator |
|
Co-Investigator(Kenkyū-buntansha) |
吉川 信也 兵庫県立大学, 生命理学研究科, 特任教授(名誉教授) (40068119)
島田 敦広 岐阜大学, 応用生物科学部, 准教授 (80723874)
|
Project Period (FY) |
2018-04-01 – 2022-03-31
|
Project Status |
Completed (Fiscal Year 2021)
|
Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2020: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
|
Keywords | チトクロムc酸化酵素 / 膜蛋白質 / 呼吸酵素 / X線結晶構造解析 / 立体構造 / プロトン能動輸送 / 酸素還元 / 生体超分子 / 膜タンパク質 / 生体エネルギー変換 / 構造と機能 / タンパク質複合体 / プロトンポンプ / チトクロム酸化酵素 |
Outline of Final Research Achievements |
Cytochrome c oxidase (CcO) reduces molecular oxygen (O2) to water, coupled with a proton pump. Electrons for the O2 reduction are transferred from cytochrome c in the positive side phase of the inner mitochondrial membrane to the O2 reduction site. The O2 reduction is performed via a catalytic cycle consisting of six stages, R, A, P, F, O and E. Four electrons are transferred from cytochrome c to CcO to reduce an O2 molecule. Each electron transfer to the O2 reduction site coupled with one proton active transfer across the mitochondrial inner-membrane. We have determined bovine CcO structures in various states to elucidate the coupling mechanism of the O2 reduction and proton pumping. In the present study structure of R-state was re-refined to improve quality of its structure, and crystal structures of A-, P-, F-, O- and E-states of CcO were successfully determined at high resolution. These structures support a proton pumping mechanism via H-pathway that has been proposed by us.
|
Academic Significance and Societal Importance of the Research Achievements |
チトクロムc酸化酵素(CcO)は呼吸鎖末端酵素で、酸素の還元とそれに同期したプロトンの能動輸送によってエネルギーを生産している。我々は長年酸素還元・プロトン能動輸送の仕組みの解明のためにウシCcOの結晶構造解析を行ってきた。 種々の反応中間体類似体等の構造解析を行い、酸素還元・プロトン能動輸送機構を提案している。この提案に対して、細菌CcOの変異体の機能解析等による多くの反論が出た。それらの反論を逐次新たな構造解析によって克服して、哺乳類に関する酸素還元・プロトン能動輸送機構としては我々の提案が認知されるようになってきた。この度の反応中間体の構造も我々の提案を一層強く支持する結果である。
|
Report
(5 results)
Research Products
(18 results)
-
-
-
-
-
-
-
-
-
[Presentation] Monomeric structure of an active form of respiratory oxygen reductase from bovine mitochondria2019
Author(s)
K. Shinzawa-Itoh, T. Sugimura, T. Misaki, Y. Tadehara, S. Yamamoto, M. Hanada, N. Yano, T. Nakagawa, S. Uene, T. Yamada, H. Aoyama, E. Yamashita, T. Tsukihara, S. Yoshikawa, K. Muramoto
Organizer
第57回日本生物物理学会年会
Related Report
-
-
-
-
-
-
-
-
-