ReviewAccounts of chemical research2025
Structural and Mechanistic Advances in the Chemistry of Methyl-Coenzyme M Reductase (MCR).
Review in Accounts of chemical research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Component A2 is a redox-sensitive archaeal ATPase activated by methyl-coenzyme M reductase.Current biology : CB · 2026Article
- Structure-activity relationship study shows versatility in substrate specificity for heterodisulfide reductase in methanogenic archaea.Protein science : a publication of the Protein Society · 2026Article
- Component A2 is a redox-sensitive archaeal ATPase activated by methyl-coenzyme M reductase.bioRxiv : the preprint server for biology · 2026Article
- Methyl coenzyme M reductase as a target for inhibition of methanogenesis in ruminants: challenges and opportunities.Frontiers in microbiology · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methane represents 34% of U.S. energy consumption and is a major greenhouse gas related to the global carbon cycle and energy production. However, current industrial practices significantly increase atmospheric methane levels, necessitating a deeper understanding of its biosynthesis and oxidation. Methyl-coenzyme M reductase (MCR) is central to biological methane metabolism, catalyzing the final step of methanogenesis and the first step in anaerobic methane oxidation. It is also a key target for strategies to capture and transform methane into value-added chemicals. The active site of MCR is a buried Ni-based cofactor only accessible by the substrates via a 50 Å long tunnel. Although the Ni(I) state is required to initiate catalysis, capturing this state remains a challenge for the current structural techniques. Recent advances in structural biology using X-ray Free-Electron Laser serial crystallography have provided insights into MCR's inactive Ni(II) state at room temperature and show promise for capturing its active Ni(I) form. Our team has established several critical aspects of the MCR mechanism using a combination of experimental and computational studies. MCR uses CH
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.