Activity inhibition mechanism of [NiFe] hydrogenase by oxidative modification of active site cysteine ligand
Project/Area Number |
16K17936
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Bio-related chemistry
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Research Institution | Nara Institute of Science and Technology |
Principal Investigator |
Tai Hulin 奈良先端科学技術大学院大学, 物質創成科学研究科, 特任助教 (40512554)
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Research Collaborator |
HIROTA Shun 奈良先端科学技術大学院大学, 物質創成科学研究科, 教授
HIGUCHI Yoshiki 兵庫県立大学, 生命理学研究科, 教授 (90183574)
XU Liyang
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Project Period (FY) |
2016-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | 金属蛋白質 / Ni酵素 / ヒドロゲナーゼ / 酸塩基平衡 / 光活性化 / 水素 / FT-IR / 生体関連化学 / タンパク質・酵素化学 |
Outline of Final Research Achievements |
[NiFe] hydrogenase catalyzes the interconversion of dihydrogen to two protons and two electrons. The acid-base equilibrium between the ready Ni-SIr and active Ni-SIa states is a common feature among [NiFe] hydrogenases, but its mechanism remains unrevealed. We have shown that the Ni-SIr state was photo-activated to its Ni-SIa state by Ar+ laser irradiation at 514.5 nm, whereas the Ni-SL state was light induced from a newly identified state, which was less active than any other identified state and existed in the “as-isolated” enzyme. Large activation energy and kinetic isotope effect were obtained for the reconversion of the Ni-SIa state to Ni-SIr state after the Ni-SIr-to-Ni-SIa photoactivation, suggesting that the Ni-SIa state reacts with H2O and leaves a bridging hydroxo ligand for the Ni-SIr state. These results provide new insights into the acid-base equilibrium of [NiFe] hydrogenase.
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Report
(3 results)
Research Products
(19 results)
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[Journal Article] Structural basis of the redox switches in the NAD+-reducing soluble [NiFe]-hydrogenase2017
Author(s)
Y. Shomura, M, Taketa, H. Nakashima, H. Tai, H. Nakagawa, Y. Ikeda, Y, M. Ishii, Y. Igarashi, H. Nishihara, K.-S. Yoon, S. Ogo, Y. Higuchi
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Journal Title
Science
Volume: 537
Issue: 6354
Pages: 928-932
DOI
Related Report
Peer Reviewed
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[Presentation] Structural and biochemical studies of Hyd-2 type [NiFe]-hydrogenase from Citrobacter sp. S-77 - proposal of the general mechanism of O2-tolerance of [NiFe]-hydrogenases2016
Author(s)
Y. Higuchi, N. D. M. Noor, H. Matsuura, K. Nishikawa, H. Nishihara, K-S.Yoon, S. Ogo, H. Tai, S. Hirota, and Y. Shomura
Organizer
11th International Hydrogenase Conference (Hydrogenase 2016)
Place of Presentation
Marseille, France
Year and Date
2016-07-13
Related Report
Int'l Joint Research / Invited
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