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Literature summary for 2.8.4.1 extracted from

  • Duin, E.C.; Signor, L.; Piskorski, R.; Mahlert, F.; Clay, M.D.; Goenrich, M.; Thauer, R.K.; Jaun, B.; Johnson, M.K.
    Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms (2004), J. Biol. Inorg. Chem., 9, 563-576.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ni contains the nickel-containing porphinoid cofactor F-430 Methanothermobacter marburgensis

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
in the silent, red1c, or ox1 states Methanothermobacter marburgensis

Synonyms

Synonyms Comment Organism
MCR
-
Methanothermobacter marburgensis
methyl-coenzyme M reductase
-
Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
F-430 nickel-containing porphinoid cofactor F-430. Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms Methanothermobacter marburgensis