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Showing content from https://link.springer.com/doi/10.1007/s007750100270 below:

The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states

Methyl-coenzyme M reductase (MCR) catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea. The enzyme contains tightly bound the nickel porphinoid F₄₃₀. The nickel enzyme has been shown to be active only when its prosthetic group is in the Ni(I) reduced state. In this state MCR exhibits the nickel-based EPR signal red1. We report here for the MCR from Methanothermobacter marburgensis that the EPR spectrum of the active enzyme changed upon addition or removal of coenzyme M, methyl coenzyme M and/or coenzyme B. In the presence of methyl-coenzyme M the red1 signal showed a more resolved ¹⁴N-superhyperfine splitting than in the presence of coenzyme M indicating a possible axial ligation of the substrate to the Ni(I). In the presence of methyl-coenzyme M and coenzyme B the red1 signal was the same as in the presence of methyl-coenzyme M alone. However, in the presence of coenzyme M and coenzyme B a highly rhombic EPR signal, MCR-red2, was induced, which was found to be light sensitive and appeared to be formed at the expense of the MCR-red1 signal. Upon addition of methyl-coenzyme M, the red2 signal disappeared and the red1 signal increased again. The red2 signal of MCR with ⁶¹Ni-labeled cofactor was significantly broadened indicating that the signal is nickel or nickel-ligand based.

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1. Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany

   Felix Mahlert, Wolfgang Grabarse, Jörg Kahnt, Rudolf K. Thauer & Evert C. Duin

1. Felix Mahlert
2. Wolfgang Grabarse
3. Jörg Kahnt
4. Rudolf K. Thauer
5. Evert C. Duin

Electronic Publication

An erratum to this article is available at http://dx.doi.org/10.1007/s00775-001-0328-9.

Mahlert, F., Grabarse, W., Kahnt, J. et al. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states. J Biol Inorg Chem 7, 101–112 (2002). https://doi.org/10.1007/s007750100270

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• Received: 23 January 2001

• Accepted: 03 June 2001

• Published: 27 July 2001

• Issue Date: January 2002

• DOI: https://doi.org/10.1007/s007750100270

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