Archives in Chemical Research Open Access

Methyl Coenzyme Reductase Reactions Involving Transient Methyl Radical Species

Akira Kobata^* Department of Chemistry, Waseda University, Japan
^*Correspondence: Akira Kobata, Department of Chemistry, Waseda University, Japan, Email:

Received: 01-Mar-2023, Manuscript No. IPACRH-23-16346; Editor assigned: 03-Mar-2023, Pre QC No. IPACRH-23-16346 (PQ); Reviewed: 17-Mar-2023, QC No. IPACRH-23-16346; Revised: 22-Mar-2023, Manuscript No. IPACRH-23-16346 (R); Published: 29-Mar-2023, DOI: 10.21767/2572-4657.7.1.10

Introduction

After methane, ethane is the second most common component of natural gas and, like methane, is chemically unreactive. Biological consumption of ethane under anaerobic conditions is suggested by geochemical profiles of marine hydrocarbon sources and ethane-dependent sulfate reduction in sludge. However, the microorganisms and reactions that catalyze this process remain unknown to this day. Other members were sulfate-reducing Deltaproteobacteria. Therefore, ethyl coenzyme was identified as an intermediate by liquid chromatography tandem mass spectrometry. Proteogenomics further suggests that the oxidation of the intermediate acetyl-coenzyme to his carbon dioxide occurs through the Wood-Ljungdahl oxidation pathway. Archaeal identification using ethane fills a gap in our knowledge of microorganisms that specifically oxidize members of the homologous alkane series in the absence of oxygen. Detection of phylogenetic and functional genetic markers associated with Ca. The Argoarchaeum of deep-sea gas vents suggests that archaea that are capable of oxidizing ethaned by ethyl-coenzyme are widespread members of the community facilitated by the release of gaseous alkanes around these vents.

Description

These consortiums are important catalysts of the global carbon cycle because of the vast amount of alkane fluxes on the seafloor. We are now cultivating a thermophilic, relatively fast-growing ethane oxidant in collaboration with sulfate-reducing bacteria known to assist in methane oxidation, making it the first short-chain alkane-degrading alkane. We’re in full production. This greatly improves our understanding of non-methanarkane activation by non-canonical methyl-coenzyme M reductase enzymes and provides insight into the mechanisms underlying additional metabolic steps and symbiotic partnerships. Ultimately, this knowledge could lead to the biotechnology development of alkanogen-producing microorganisms to support CO₂ neutrality in industrial processes.

The methyl coenzyme M reductase was originally identified as the final step catalyst of the methanogenesis pathway. Anaerobic methane-oxidizing archaea were discovered that use methyl coenzyme M reductase enzymes to activate methane. Anaerobic methane-oxidizing archaea thrives at the thermodynamic limit of life, grows slowly, and most often forms symbiotic consortia with sulfate-reducing bacteria. Recently, archaea that are capable of anaerobically oxidizing non-methane polycarbon alkanes such as ethane and n-butane have been reported in both enriched cultures and environmental samples. Presenting a detailed Methyl coenzyme M reductase/alkyl coenzyme M reductase-based phylogeny, compare their metabolic pathways, and discuss knowledge gaps in the physiology of these organisms to explore the diversity, distribution, and function of Anaerobic methane-oxidizing archaea and alkane-oxidizing archaea. Methyl coenzyme M reductase contains the nickel hydrocorfinoid cofactor and is an essential enzyme that catalyzes anaerobic methane production and oxidation. The active Nickel species of the methyl coenzyme M reductase convert methyl coenzyme M and coenzyme to methane and heterodisulfides [1-4].

Conclusion

A mechanism has been proposed. In parallel with studies of the native Methyl coenzyme M reductase itself, Methyl coenzyme M reductase function was investigated in the context of new protein-based functional models. In the latter case, hemproteins reconstituted with tetradehydro and didehydrocorrinoid nickel complexes proved to be useful model systems responsible for methanogenesis. These efforts support the proposed enzymatic reaction mechanism and provide important insights into the replication of Methyl coenzyme M reductase like methanogenic processes.

Acknowledgement

None.

Conflict of Interest

Authors declare no conflict of interest.

References

1. Hurtado M, Davidson JL, Blyth CA, Lowe J (2010) Holographic detection of hydrocarbon gases and other volatile organic compounds. Langmuir. 26(19): 15694-9.

   [Crossref] [Google Scholar] [Pubmed]

2. Piliang H, Sunil S, Adav D (2017) Recent advances in mass spectrometric analysis of protein deamidation. Mass Spectrom Rev. 36(6): 677-692.

   [Crossref] [Google Scholar] [Pubmed]

3. Sun J, Geng Z, Xue N (2018) A mini-system integrated with metal-oxide-semiconductor sensor and micro-packed gas chromatographic column. Micromachines. 9(8): 408.

   [Crossref] [Google Scholar] [Pubmed]

4. Noyhouzer T, Valdinger I, Mandler D (2013) Enhanced potentiometry by metallic nanoparticles. Anal Chem. 85(17): 8347-8353.

   [Crossref] [Google Scholar] [Pubmed]