ArticleJournal of bacteriology2014
Elucidating the process of activation of methyl-coenzyme M reductase.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.
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Who cites it
30 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A meta-analysis of effects of 3-nitrooxypropanol on methane production, yield, and intensity in dairy cattle.Journal of dairy science · 2023Pooled it
- Diversity of electron-bifurcating COScience advances · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Component A2 is a redox-sensitive archaeal ATPase activated by methyl-coenzyme M reductase.Current biology : CB · 2026Article
- Component A2 is a redox-sensitive archaeal ATPase activated by methyl-coenzyme M reductase.bioRxiv : the preprint server for biology · 2026Article
- Short- and long-term dietary supplementation as well as withdrawal of the enteric methane inhibitor 3-nitrooxypropanol reveal distinct effects on the rumen microbial community.Journal of animal science and biotechnology · 2025Article
- Salvianolic acid C inhibits methane emissions in dairy cows by targeting MCR and reshaping the rumen microbial community.Journal of animal science and biotechnology · 2025Article
- Methanogenesis inhibition remodels microbial fermentation and stimulates acetogenesis in ruminants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Simulated early Earth geochemistry fuels a hydrogen-dependent primordial metabolism.Nature ecology & evolution · 2025Article
- Navigating the Complex Terrain of Methane Synthesis: Multienzyme Control Points and Data-Driven Strategies.ACS omega · 2025Article
- Methyl coenzyme M reductase as a target for inhibition of methanogenesis in ruminants: challenges and opportunities.Frontiers in microbiology · 2025Review
- Impact of mineral and non-mineral sources of iron and sulfur on the metalloproteome ofApplied and environmental microbiology · 2024Article
- The crystal structure of methanogen McrD, a methyl-coenzyme M reductase-associated protein.FEBS open bio · 2024Article
- McrD binds asymmetrically to methyl-coenzyme M reductase improving active-site accessibility during assembly.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Reactivity Factors in Catalytic Methanogenesis and Their Tuning upon Coenzyme F430 Biosynthesis.Journal of the American Chemical Society · 2023Article
- The origin and evolution of methanogenesis andPNAS nexus · 2023Article
- Effect of 3-nitrooxypropanol on enteric methane emissions of feedlot cattle fed with a tempered barley-based diet with canola oil.Journal of animal science · 2023Article
- Genomic remnants of ancestral methanogenesis and hydrogenotrophy in Archaea drive anaerobic carbon cycling.Science advances · 2022Article
- Expression of divergent methyl/alkyl coenzyme M reductases from uncultured archaea.Communications biology · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methyl-coenzyme M reductase (MCR) catalyzes the reversible reduction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methane and heterodisulfide CoM-S-S-CoB (HDS). MCR contains the hydroporphinoid nickel complex coenzyme F430 in its active site, and the Ni center has to be in its Ni(I) valence state for the enzyme to be active. Until now, no in vitro method that fully converted the inactive MCRsilent-Ni(II) form to the active MCRred1-Ni(I) form has been described. With the potential use of recombinant MCR in the production of biofuels and the need to better understand this enzyme and its activation process, we studied its activation under nonturnover conditions and achieved full MCR activation in the presence of dithiothreitol and protein components A2, an ATP carrier, and A3a. It was found that the presence of HDS promotes the inactivation of MCRred1, which makes it essential that the activation process is isolated from the methane formation assay, which tends to result in minimal activation rates. Component A3a is a multienzyme complex that includes the mcrC gene product, an Fe-protein homolog, an iron-sulfur flavoprotein, and protein components involved in electron bifurcation. A hypothetical model for the cellular activation process of MCR is presented.
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