ArticleProceedings of the National Academy of Sciences of the United States of America2020
Small protein folds at the root of an ancient metabolic network.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- The Ascent of Miniproteins.Biochemistry · 2026Review
- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
- Protein folds and catalytic strategies at the origin of biological CO2 fixation.FEMS microbiology ecology · 2026Article
- Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026Article
- Article
- Comparative Dynamics Enables Discovery of Embedded Bacterial Ferredoxin Domains in Large Redox Enzymes.Proteins · 2025Article
- Science of the gaps.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- The ability of pentose pathways to form all essential metabolites provides clues to the origins of metabolism.PLoS biology · 2025Article
- Reused Protein Segments Linked to Functional Dynamics.Molecular biology and evolution · 2024Article
- The crystal structure of methanogen McrD, a methyl-coenzyme M reductase-associated protein.FEBS open bio · 2024Article
- Unveiling the role of inorganic nanoparticles in Earth's biochemical evolution through electron transfer dynamics.iScience · 2024Review
- Reflections on the Origin of Coded Protein Biosynthesis.Biomolecules · 2024Review
- Structures and Electron Transport Paths in the Four Families of Flavin-Based Electron Bifurcation Enzymes.Sub-cellular biochemistry · 2024Review
- Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology.Frontiers in chemistry · 2024Review
- Back in time to the Gly-rich prototype of the phosphate binding elementary function.Current research in structural biology · 2024Review
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Prebiotic Synthesis of ATP: A Terrestrial Volcanism-Dependent Pathway.Life (Basel, Switzerland) · 2023Article
- Metals in Prebiotic Catalysis: A Possible Evolutionary Pathway for the Emergence of Metalloproteins.ACS omega · 2023Review
- Is biofilm formation intrinsic to the origin of life?Environmental microbiology · 2023Article
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5 authors.
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Abstract
Life on Earth is driven by electron transfer reactions catalyzed by a suite of enzymes that comprise the superfamily of oxidoreductases (Enzyme Classification EC1). Most modern oxidoreductases are complex in their structure and chemistry and must have evolved from a small set of ancient folds. Ancient oxidoreductases from the Archean Eon between ca. 3.5 and 2.5 billion years ago have been long extinct, making it challenging to retrace evolution by sequence-based phylogeny or ancestral sequence reconstruction. However, three-dimensional topologies of proteins change more slowly than sequences. Using comparative structure and sequence profile-profile alignments, we quantify the similarity between proximal cofactor-binding folds and show that they are derived from a common ancestor. We discovered that two recurring folds were central to the origin of metabolism: ferredoxin and Rossmann-like folds. In turn, these two folds likely shared a common ancestor that, through duplication, recruitment, and diversification, evolved to facilitate electron transfer and catalysis at a very early stage in the origin of metabolism.
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