Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
- 22 April 2005
- journal article
- Published by Springer Science and Business Media LLC in JBIC Journal of Biological Inorganic Chemistry
- Vol. 10 (4), 333-342
- https://doi.org/10.1007/s00775-005-0636-6
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analoguesJBIC Journal of Biological Inorganic Chemistry, 2004
- Spectroscopic investigation of the nickel-containing porphinoid cofactor F430. 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 formsJBIC Journal of Biological Inorganic Chemistry, 2004
- Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formationJBIC Journal of Biological Inorganic Chemistry, 2003
- The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2JBIC Journal of Biological Inorganic Chemistry, 2002
- The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 statesJBIC Journal of Biological Inorganic Chemistry, 2001
- On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate bindingJournal of Molecular Biology, 2001
- Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptationJournal of Molecular Biology, 2000
- On the role of N‐7‐mercaptoheptanoyl‐O‐phospho‐L‐threonine (component B) in the enzymatic reduction of methyl‐coenzyme M to methaneFEBS Letters, 1987
- The L‐form of N‐7‐mercaptoheptanoyl‐O‐phosphothreonine is the enantiomer active as component B in methyl‐CoM reduction to methaneFEBS Letters, 1987
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976