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Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F-420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family

MPS-Authors
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Aufhammer,  S. W.
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Warkentin,  E.
Max Planck Society;

Ermler,  U.
Max Planck Society;

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Hagemeier,  C. H.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  R. K.
Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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

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Citation

Aufhammer, S. W., Warkentin, E., Ermler, U., Hagemeier, C. H., Thauer, R. K., & Shima, S. (2005). Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F-420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family. Protein Science, 14(7), 1840-1849.


Cite as: http://hdl.handle.net/21.11116/0000-0007-C835-C
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