The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron 
ligation in the active site iron complex

Hiromoto, Takeshi; Ataka, Kenichi; Pilak, Oliver; Vogt, Sonja; Stagni, Marco Salomone; Meyer-Klaucke, Wolfram; Warkentin, Eberhard; Thauer, Rudolf Kurt; Shima, Seigo; Ermler, Ulrich

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The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex

Hiromoto, T., Ataka, K., Pilak, O., Vogt, S., Stagni, M. S., Meyer-Klaucke, W., et al. (2009). The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Letters, 583(3), 585-590.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-C4D5-B Version Permalink: https://hdl.handle.net/21.11116/0000-0007-C4D6-A

Genre: Journal Article

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Creators:
Hiromoto, Takeshi¹, Author
Ataka, Kenichi, Author
Pilak, Oliver¹, Author
Vogt, Sonja¹, Author
Stagni, Marco Salomone, Author
Meyer-Klaucke, Wolfram, Author
Warkentin, Eberhard², Author
Thauer, Rudolf Kurt³, Author
Shima, Seigo⁴, Author
Ermler, Ulrich², Author

Affiliations:
1Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311
2Max Planck Society, ou_persistent13
3Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266289
4Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277

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Language(s): eng - English

Dates: Date issued: 2009

Publication Status: Issued

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Identifiers: eDoc: 443430

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Title: FEBS Letters

Source Genre: Journal

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Pages: - Volume / Issue: 583 (3) Sequence Number: - Start / End Page: 585 - 590 Identifier: -