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Journal Article

Characterization of a heme-dependent catalase from Methanobrevibacter arboriphilus

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/persons/resource/persons254714

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

Sordel-Klippert,  M
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254760

Thauer,  Rudolf K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Shima, S., Sordel-Klippert, M., Brioukhanov, A., Netrusov, A., Linder, D., & Thauer, R. K. (2001). Characterization of a heme-dependent catalase from Methanobrevibacter arboriphilus. Applied and Environmental Microbiology, 67(7), 3041-3045. doi:10.1128/AEM.67.7.3041-3045.2001.


Cite as: https://hdl.handle.net/21.11116/0000-0009-440E-C
Abstract
Recently it was reported that methanogens of the genus Methanobrevibacter exhibit catalase activity. This was surprising, since Methanobrevibacter species belong to the order Methanobacteriales, which are known not to contain cytochromes and to lack the ability to synthesize heme, We report here that Methanobrevibacter arboriphilus strains AZ and DH1 contained catalase activity only when the growth medium was supplemented with hemin. The heme catalase was purified and characterized, and the encoding gene was cloned. The amino acid sequence of the catalase from the methanogens is most similar to that of Methanosarcina barkeri.