Structural chemistry of O2-tolerant [NiFe]-hydrogenases
Project/Area Number |
25291038
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | University of Hyogo |
Principal Investigator |
Higuchi Yoshiki 兵庫県立大学, 生命理学研究科, 教授 (90183574)
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥17,680,000 (Direct Cost: ¥13,600,000、Indirect Cost: ¥4,080,000)
Fiscal Year 2015: ¥7,410,000 (Direct Cost: ¥5,700,000、Indirect Cost: ¥1,710,000)
Fiscal Year 2014: ¥7,410,000 (Direct Cost: ¥5,700,000、Indirect Cost: ¥1,710,000)
Fiscal Year 2013: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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Keywords | X線結晶解析 / 酸素耐性酵素 / Ni酵素 / ヒドロゲナーゼ / 燃料電池 / 中性子結晶解析 / 反応機構 / プロトンチャネル / 中性子解析 |
Outline of Final Research Achievements |
In this study, x-ray structure analysis of newly found O2-tolerant [NiFe]-hydrogenase and neutron structure analysis of standard enzyme have been carried out. 1. The x-ray structures of the newly found O2-tolerant [NiFe]-hydrogenase from Citrobacter sp. S-77 in the air-oxidized, K3Fe(CN)6-oxidized and H2-reduced forms have been successfully solved at the resolutions better than 2.0 A. The one of the iron-sulfur clusters (the proximal to the Ni-Fe active site) is not a [4Fe3S]-type, which was found in the usual O2-tolerant enzymes, but a [4Fe4S]-type typical as those in the standard enzymes. This [4Fe4S]-type cluster changed its structure when the enzyme is oxidized by K3Fe(CN)6, but the mechanism of the structural changed are different from those clusters in O2-tolerant hydrogenase. 2. Neutron diffraction data up to 2.0 A resolution have been successfully obtained from a large crystal (>1.5 mm3) grown in D2O.
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Report
(4 results)
Research Products
(98 results)
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[Journal Article] “Newton’s cradle” proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography2015
Author(s)
Nakamura, A., Ishida, T., Kusaka, K., Yamada, T., Fushinobu, S., Tanaka, I., Kaneko, S., Ohta, K., Tanaka, H., Inaka, K., Higuchi, Y., Niimura, N., Samejima, M., and Igarashi, K.
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Journal Title
Science Adv.
Volume: 1
Issue: 7
DOI
NAID
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Crystallization and preliminary X-ray analysis of the NAD+-reducing [NiFe] hydrogenase from Hydrogenophilus thermoluteolus TH-1.2015
Author(s)
Taketa M, Nakagawa H, Habukawa M, Osuka H, Kihira K, Komori H, Shibata N, Ishii M, Igarashi Y, Nishihara H, Yoon KS, Ogo S, Shomura Y, Higuchi Y.
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Journal Title
Acta Crystallogr F Struct Biol Commun.
Volume: 71
Issue: 1
Pages: 96-99
DOI
Related Report
Peer Reviewed
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[Journal Article] Studies on hydrogenase2013
Author(s)
T. Yagi, Y. Higuchi
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Journal Title
Proceedings of the Japan Academy, Series B
Volume: 89
Issue: 1
Pages: 16-33
DOI
NAID
ISSN
0386-2208, 1349-2896
Related Report
Peer Reviewed
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[Journal Article] Crystallization and X-ray diffraction analysis of nylon hydrolase (NylC) from Arthrobacter sp2013
Author(s)
Nagai, K., Yasuhira, K., Tanaka, Y., Kato, D., Takeo, M., Higuchi, Y., Negoro, S., & Shibata N.
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Journal Title
KI72 Acta Cryst.
Volume: F69
Issue: 10
Pages: 1151-1154
DOI
Related Report
Peer Reviewed
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[Presentation] Purification and Crystallization of NAD+-reducing [NiFe]-hydrogenase2014
Author(s)
H. Nakagawa, M. Taketa, M. Habukawa, K. Kihira, N. Shibata, H. Nishihara, K.-S. Yoon, S. Ogo, Ma. Ishii, Y. Igarashi, Y. Shomura and Y. Higuchi
Organizer
第1回ピコバイロジー研究所国際シンポジウム
Place of Presentation
理研XFEL大会議室(兵庫)
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