ArticleFrontiers in microbiology2013
In vivo activation of methyl-coenzyme M reductase by carbon monoxide.
Article in Frontiers in microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.
- A meta-analysis of effects of 3-nitrooxypropanol on methane production, yield, and intensity in dairy cattle.Journal of dairy science · 2023Pooled it
- 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
- Article
- 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
- Overview of Diverse Methyl/Alkyl-Coenzyme M Reductases and Considerations for Their Potential Heterologous Expression.Frontiers in microbiology · 2022Review
- Methyl-Coenzyme M Reductase and Its Post-translational Modifications.Frontiers in microbiology · 2020Review
- Review
- Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Proteomic Analysis of the Hydrogen and Carbon Monoxide Metabolism of Methanothermobacter marburgensis.Frontiers in microbiology · 2016Article
- The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order.The Journal of biological chemistry · 2015Article
- Elucidating the process of activation of methyl-coenzyme M reductase.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methyl-coenzyme M reductase (MCR) from methanogenic archaea catalyzes the rate-limiting and final step in methane biosynthesis. Using coenzyme B as the two-electron donor, MCR reduces methyl-coenzyme M (CH3-SCoM) to methane and the mixed disulfide, CoBS-SCoM. MCR contains an essential redox-active nickel tetrahydrocorphinoid cofactor, Coenzyme F430, at its active site. The active form of the enzyme (MCRred1) contains Ni(I)-F430. Rapid and efficient conversion of MCR to MCRred1 is important for elucidating the enzymatic mechanism, yet this reduction is difficult because the Ni(I) state is subject to oxidative inactivation. Furthermore, no in vitro methods have yet been described to convert Ni(II) forms into MCRred1. Since 1991, it has been known that MCRred1 from Methanothermobacter marburgensis can be generated in vivo when cells are purged with 100% H2. Here we show that purging cells or cell extracts with CO can also activate MCR. The rate of in vivo activation by CO is about 15 times faster than by H2 (130 and 8 min(-1), respectively) and CO leads to twofold higher MCRred1 than H2. Unlike H2-dependent activation, which exhibits a 10-h lag time, there is no lag for CO-dependent activation. Based on cyanide inhibition experiments, carbon monoxide dehydrogenase is required for the CO-dependent activation. Formate, which also is a strong reductant, cannot activate MCR in M. marburgensis in vivo.
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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.