Biosynthesis of the Iron-Guanylylpyridinol Cofactor of [Fe]-Hydrogenase in Methanogenic Archaea as Elucidated by Stable-Isotope Labeling-Reference-Cited by-同舟云学术

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Biosynthesis of the Iron-Guanylylpyridinol Cofactor of [Fe]-Hydrogenase in Methanogenic Archaea as Elucidated by Stable-Isotope Labeling

Published:2012-02-06 Issue:6 Volume:134 Page:3271-3280
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Schick Michael¹,Xie Xiulan²,Ataka Kenichi³,Kahnt Jörg¹,Linne Uwe²,Shima Seigo¹⁴

Affiliation:

1. Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse 10, 35043 Marburg, Germany

2. Department of Chemistry, Philipps-Universität Marburg, Hans-Meerwein Strasse, 35032 Marburg, Germany

3. Department of Physics, Freie-Universität Berlin, Arnimallee 14, 14195 Berlin, Germany

4. PRESTO, Japan Science and Technology Agency (JST), Honcho, Kawaguchi, Saitama 332-0012, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja211594m

Reference56 articles.

1. Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H2 Storage

2. UNUSUAL COENZYMES OF METHANOGENESIS

3. H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea

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

5. The Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H2Activation

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