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

MPS-Authors
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Hiromoto,  Takeshi
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Pilak,  Oliver
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Vogt,  Sonja
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Warkentin,  Eberhard
Max Planck Society;

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Thauer,  Rudolf Kurt
Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Ermler,  Ulrich
Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0007-C4D5-B
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