Methyl-coenzyme M reductase (MCR) catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea. The enzyme has two structurally interlinked active sites embedded in an α2β2γ2 subunit structure. Each active site has the nickel porphyrinoid F430 as a prosthetic group. In the active state, F430 contains the transition metal in the Ni(I) oxidation state. The active enzyme exhibits an axial Ni(I)-based continuous wave (CW) electron paramagnetic resonance (EPR) signal, called red1a in the absence of substrates or red1c in the presence of coenzyme M. Addition of coenzyme B to the MCR-red1 state can partially and reversibly convert it into the MCR-red2 form, which shows a rhombic Ni(I)-based EPR signal (at X-band microwave frequencies of approximately 9.4 GHz). In this report we present evidence from high-field/high-frequency CW EPR spectroscopy (W-band, microwave frequency of approximately 94 GHz) that the red2 state consists of two substates that could not be resolved by EPR spectroscopy at X-band frequencies. At W-band it becomes apparent that upon addition of coenzyme B to MCR in the red1c state, two red2 EPR signals are induced, not one as was previously believed. The first signal is the well-characterized (ortho)rhombic EPR signal, thus far called red2, while the second previously unidentified signal is axial. We have named the two substates MCR-red2r and MCR-red2a after their rhombic and axial signals, respectively.
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Similar content being viewed by others Explore related subjectsDiscover the latest articles and news from researchers in related subjects, suggested using machine learning. AbbreviationsMethyl-coenzyme M
Continuous wave
Electron paramagnetic resonance
Coenzyme B
Coenzyme M
Hyperfine sublevel correlation
Methyl-coenzyme M reductase
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We thank the Swiss National Science Foundation (SNF) and the Fonds der Chemischen Industrie for financial support. D.H. gratefully acknowledges a research scholarship (HI 1094/1-1) from the Deutsche Forschungsgemeinschaft (DFG).
Author information Authors and AffiliationsLaboratorium für Physikalische Chemie, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
Denise I. Kern, Jeffrey Harmer & Dariush Hinderberger
Max-Planck-Institut für Polymerforschung, Ackermannweg 10, 55128, Mainz, Germany
Dariush Hinderberger
Laboratorium für Organische Chemie, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
Bernhard Jaun
Max-Planck-Institut für Terrestrische Mikrobiologie, Karl-von-Frisch-Straße, 35043, Marburg, Germany
Meike Goenrich & Rudolf K. Thauer
Correspondence to Dariush Hinderberger.
Electronic supplementary materialBelow is the link to the electronic supplementary material.
About this article Cite this articleKern, D.I., Goenrich, M., Jaun, B. et al. Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy. J Biol Inorg Chem 12, 1097–1105 (2007). https://doi.org/10.1007/s00775-007-0281-3
Received: 18 May 2007
Accepted: 18 July 2007
Published: 10 August 2007
Issue Date: November 2007
DOI: https://doi.org/10.1007/s00775-007-0281-3
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