ArticleThe Journal of biological chemistry2015
The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 58 citations in OpenAlex.
- In Vitro Evaluation of Spearmint Essential Oil (Animals : an open access journal from MDPI · 2026Article
- Uncovering Major Structural and Functional Features of Methyl-Coenzyme M Reductase (MCR) fromInternational journal of molecular sciences · 2026Article
- Anti-methanogenic effect of phytogenic extract ofJournal of advanced veterinary and animal research · 2025Article
- Structural and Mechanistic Advances in the Chemistry of Methyl-Coenzyme M Reductase (MCR).Accounts of chemical research · 2025Review
- Methyl coenzyme M reductase as a target for inhibition of methanogenesis in ruminants: challenges and opportunities.Frontiers in microbiology · 2025Review
- The effect ofMicrobiology spectrum · 2024Article
- A diversified, widespread microbial gene cluster encodes homologs of methyltransferases involved in methanogenesis.bioRxiv : the preprint server for biology · 2023Article
- A Structural View of Alkyl-Coenzyme M Reductases, the First Step of Alkane Anaerobic Oxidation Catalyzed by Archaea.Biochemistry · 2022Review
- XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase.Journal of inorganic biochemistry · 2022Article
- Repurposing metalloproteins as mimics of natural metalloenzymes for small-molecule activation.Journal of inorganic biochemistry · 2021Review
- Catalytic activity regulation through post-translational modification: the expanding universe of protein diversity.Advances in protein chemistry and structural biology · 2020Review
- Methyl-Coenzyme M Reductase and Its Post-translational Modifications.Frontiers in microbiology · 2020Review
- Trace Metal Availability Affects Greenhouse Gas Emissions and Microbial Functional Group Abundance in Freshwater Wetland Sediments.Frontiers in microbiology · 2020Article
- Review
- Methane and Inflammation - A Review (Fight Fire with Fire).Intensive care medicine experimental · 2019Review
- Energy Conservation and Hydrogenase Function in Methanogenic Archaea, in Particular the GenusMicrobiology and molecular biology reviews : MMBR · 2019Review
- An evolving view of methane metabolism in the Archaea.Nature reviews. Microbiology · 2019Review
- Plane of nutrition affects the phylogenetic diversity and relative abundance of transcriptionally active methanogens in the bovine rumen.Scientific reports · 2017Article
- Article
- Biocatalysts for methane conversion: big progress on breaking a small substrate.Current opinion in chemical biology · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methyl-coenzyme M reductase (MCR) is a nickel tetrahydrocorphinoid (coenzyme F430) containing enzyme involved in the biological synthesis and anaerobic oxidation of methane. MCR catalyzes the conversion of methyl-2-mercaptoethanesulfonate (methyl-SCoM) and N-7-mercaptoheptanoylthreonine phosphate (CoB7SH) to CH4 and the mixed disulfide CoBS-SCoM. In this study, the reaction of MCR from Methanothermobacter marburgensis, with its native substrates was investigated using static binding, chemical quench, and stopped-flow techniques. Rate constants were measured for each step in this strictly ordered ternary complex catalytic mechanism. Surprisingly, in the absence of the other substrate, MCR can bind either substrate; however, only one binary complex (MCR·methyl-SCoM) is productive whereas the other (MCR·CoB7SH) is inhibitory. Moreover, the kinetic data demonstrate that binding of methyl-SCoM to the inhibitory MCR·CoB7SH complex is highly disfavored (Kd = 56 mM). However, binding of CoB7SH to the productive MCR·methyl-SCoM complex to form the active ternary complex (CoB7SH·MCR(Ni(I))·CH3SCoM) is highly favored (Kd = 79 μM). Only then can the chemical reaction occur (kobs = 20 s(-1) at 25 °C), leading to rapid formation and dissociation of CH4 leaving the binary product complex (MCR(Ni(II))·CoB7S(-)·SCoM), which undergoes electron transfer to regenerate Ni(I) and the final product CoBS-SCoM. This first rapid kinetics study of MCR with its natural substrates describes how an enzyme can enforce a strictly ordered ternary complex mechanism and serves as a template for identification of the reaction intermediates.
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