Literature summary for 2.8.4.1 extracted from

Goenrich, M.; Duin, E.C.; Mahlert, F.; Thauer, R.K.
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B (2005), J. Biol. Inorg. Chem., 10, 333-342.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ni	the niuckel porphinoid F-430 must be in the Ni(I) oxidation state for the enzyme to be active. The active enzyme exhibits an axial Ni(I)-based electron paramagnetic resonance signal and a UV-vis spectrum with an absorption maximum at 385 nM. This state is called the MCR-red1 state. When the temperature is lowered below 20°C the perecentage of MCR in the red2 state decreases and that in the red1 state increases. These changes with temperature are fully reversible. At most 50% of the enzyme is converted to the MCR-red2 state under all experimental conditions	Methanothermobacter marburgensis

Organism

Organism	UniProt	Comment	Textmining
Methanothermobacter marburgensis	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
F-430	prosthetic group	Methanothermobacter marburgensis

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Release 2023.1 (January 2023)