An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea

Künkel, Andreas; Vorholt, Julia A.; Thauer, Rudolf K.; Hedderich, Reiner

doi:10.1046/j.1432-1327.1998.2520467.x

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An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea

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Künkel, Andreas
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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Vorholt, Julia A.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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Thauer, Rudolf K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

Hedderich, Reiner
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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https://doi.org/10.1046/j.1432-1327.1998.2520467.x
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Citation

Künkel, A., Vorholt, J. A., Thauer, R. K., & Hedderich, R. (1998). An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea. European Journal of Biochemistry, 252(3), 467-476. doi:10.1046/j.1432-1327.1998.2520467.x.

Cite as: https://hdl.handle.net/21.11116/0000-000F-ACE0-2

Abstract

Methanogenic archaea are known to contain two types of [NiFe]
hydrogenases designated F(420)-reducing hydrogenase and
F(420)-non-reducing hydrogenase. We report here that they additionally
contain Escherichia coli hydrogenase-3-type [NiFe] hydrogenases. The
evidence is based on biochemical studies and analysis of the subunit
primary structure of this hydrogenase (designated Ech) purified from
membranes of acetate-grown cells of Methanosarcina barkeri. The subunits
EchE and EchC of the EchABCDEF complex showed 34% and 45% sequence
identity to the nickel-containing large subunit HycE and to the
iron-sulfur cluster containing small subunit HycG, respectively, of the
hydrogenase in the formate hydrogen lyase complex from E. coli. Analysis
of the totally sequenced genomes of Methanococcus jannaschii and
Methanobacterium thermoautotrophicum strain Delta H revealed that these
organisms contain similar open reading frames, indicating the presence
of an E. coli hydrogenase-3-type hydrogenase also in these methanogenic
archaea.