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ATP-Driven Structure Activates Methyl-Coenzyme M Reductase
- A recent study published in Nature unravels the evolution and structural complexities of the ATP-driven methyl-coenzyme M reductase (MCR) activation complex, shedding light on iron-sulfur clusters in archaic enzymatic systems.
- The research challenges previous assumptions about the unique presence of [8Fe-9S-C] clusters in the nitrogenase (Nif) family, suggesting a broader and earlier evolutionary distribution starting with methanogenic archaea.
- MCR is a crucial enzyme in methanogenesis, and the activation process involving iron-sulfur clusters has been a biological puzzle, now better understood through this study.
- The study reconstructs the evolutionary history of [8Fe-9S-C] clusters, indicating their initial presence in MCR systems before being adopted by nitrogenase enzymes involved in nitrogen fixation.
- By employing advanced phylogenomic techniques, the researchers traced the presence of [8Fe-9S-C] cluster-binding proteins McrC and Mmp7 across ancient archaeal lineages, showing their deep-rooted distribution.
- Phylogenetic analyses suggest that these clusters were present in the common ancestor of key archaeal groups, enhancing the understanding of MCR's antiquity in methanogenic archaea.
- The study also explores the evolution of NifB and CfbD enzymes, revealing complex gene duplications and transfers that led to the diverse nitrogenase enzymes observed today.
- The findings indicate that the [8Fe-9S-C] cluster's primary use likely originated in MCR activation before being acquired by nitrogenase systems, showcasing an evolutionary repurposing of metalloclusters.
- This research not only reshapes our knowledge of enzymatic cofactors but also provides insights into early archaeal electron transfer mechanisms and bioenergetics in extreme environments.
- The study's interdisciplinary approach highlights the power of integrating structural biology and computational phylogenetics to elucidate deep evolutionary secrets and revisit enzymatic function through a molecular evolution lens.
- Overall, the identification of ancient [8Fe-9S-C] clusters in the MCR activation complex revolutionizes our understanding of metallocluster utilization and evolutionary innovation, offering implications for bioengineering applications.
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