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

doi:10.1016/j.febslet.2009.01.017

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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. doi:10.1016/j.febslet.2009.01.017.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-C4D5-B Version Permalink: https://hdl.handle.net/21.11116/0000-000F-B509-B

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https://doi.org/10.1016/j.febslet.2009.01.017 (Publisher version) Open Access Hybrid

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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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Abstract: [Fe]-hydrogenase is one of three types of enzymes known to activate H(2). Crystal structure analysis recently revealed that its active site iron is ligated square-pyramidally by Cys176-sulfur, two CO, an "unknown" ligand and the sp(2)-hybridized nitrogen of a unique iron-guanylylpyridinol-cofactor. We report here on the structure of the C176A mutated enzyme crystallized in the presence of dithiothreitol (DTT). It suggests an iron center octahedrally coordinated by one DTT-sulfur and one DTT-oxygen, two CO, the 2-pyridinol's nitrogen and the 2-pyridinol's 6-formylmethyl group in an acyl-iron ligation. This result led to a re-interpretation of the iron ligation in the wild-type.

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Language(s): eng - English

Dates: Date issued: 2009-01-20

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 443430
DOI: 10.1016/j.febslet.2009.01.017

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Title: FEBS Letters

Other : FEBS Lett.

Source Genre: Journal

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Publ. Info: Amsterdam : Elsevier

Pages: - Volume / Issue: 583 (3) Sequence Number: - Start / End Page: 585 - 590 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501