PREPARATION OF [FE]-HYDROGENASE FROM METHANOGENIC ARCHAEA

Shima, S.; Schick, M.; Tamura, H.

doi:10.1016/b978-0-12-385112-3.00007-x

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PREPARATION OF [FE]-HYDROGENASE FROM METHANOGENIC ARCHAEA

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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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Schick, M.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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

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Citation

Shima, S., Schick, M., & Tamura, H. (2011). PREPARATION OF [FE]-HYDROGENASE FROM METHANOGENIC ARCHAEA. Methods in Enzymology, (494), 119-137. doi:10.1016/b978-0-12-385112-3.00007-x.

Cite as: https://hdl.handle.net/21.11116/0000-0007-C2C7-D

Abstract

[Fe]-hydrogenase is one of the three types of hydrogenases. This enzyme is found in many hydrogenotrophic methanogenic archaea and catalyzes the reversible hydride transfer from H(2) to methenyl-H(4)MPT(+) in methanogenesis from H(2) and CO(2). The enzyme harbors a unique iron-guanylyl pyridinol (FeGP) cofactor as a prosthetic group. Here, we describe the purification of [Fe]-hydrogenase from Methanothermobacter marburgensis, the isolation of the FeGP cofactor from the native holoenzyme, and the reconstitution of [Fe]-hydrogenase from the isolated FeGP cofactor and the heterologously produced apoenzyme.