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  The Iron-Sulfur Cluster-free Hydrogenase (Hmd) Is a Metalloenzyme with a Novel Iron Binding Motif.

Korbas, M., Vogt, S., Meyer-Klaucke, W., Bill, E., Lyon, E., Thauer, R., & Shima, S. (2006). The Iron-Sulfur Cluster-free Hydrogenase (Hmd) Is a Metalloenzyme with a Novel Iron Binding Motif. J. Biol. Chem., 281, 30804-13. doi:10.1074/jbc.m605306200.

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アイテムのパーマリンク: https://hdl.handle.net/21.11116/0000-0007-C737-B 版のパーマリンク: https://hdl.handle.net/21.11116/0000-0009-4B03-0
資料種別: 学術論文

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 作成者:
Korbas, Malgorzata, 著者
Vogt, Sonja1, 著者           
Meyer-Klaucke, Wolfram, 著者
Bill, Eckhard, 著者
Lyon, Erica1, 著者           
Thauer, Rudolf2, 著者           
Shima, Seigo3, 著者           
所属:
1Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311              
2Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266289              
3Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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 要旨: The iron-sulfur cluster-free hydrogenase (Hmd) from methanogenic archaea harbors an iron-containing cofactor of yet unknown structure. X-ray absorption spectroscopy of the active, as isolated enzyme from Methanothermobacter marburgensis (mHmd) and of the active, reconstituted enzyme from Methanocaldococcus jannaschii (jHmd) revealed the presence of mononuclear iron with two CO, one sulfur and one or two N/O in coordination distance. In jHmd, the single sulfur ligand is most probably provided by Cys176, as deduced from a comparison of the activity and of the x-ray absorption and Mössbauer spectra of the enzyme mutated in any of the three conserved cysteines. In the isolated Hmd cofactor, two CO, one sulfur, and two nitrogen/oxygen atoms coordinate the iron, the sulfur ligand being most probably provided by mercaptoethanol, which is absolutely required for the extraction of the iron-containing cofactor from the holoenzyme and for the stabilization of the extracted cofactor. In active mHmd holoenzyme, the number of iron ligands increased by one when one of the Hmd inhibitors (CO or KCN) were present, indicating that in active Hmd, the iron contains an open coordination site, which is proposed to be the site of H2 interaction.

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言語: eng - English
 日付: 2006-08-03
 出版の状態: 出版
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 査読: -
 識別子(DOI, ISBNなど): eDoc: 298222
DOI: 10.1074/jbc.m605306200
 学位: -

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出版物 1

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出版物名: J. Biol. Chem.
種別: 学術雑誌
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出版社, 出版地: -
ページ: - 巻号: 281 通巻号: - 開始・終了ページ: 30804 - 13 識別子(ISBN, ISSN, DOIなど): -