ArticleScience advances2022
Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- The Ascent of Miniproteins.Biochemistry · 2026Review
- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
- Coenzyme-protein interactions since early life.eLife · 2025Article
- Interpretable prediction of zinc ion location in proteins with ZincSight.Protein science : a publication of the Protein Society · 2025Article
- Comparative Dynamics Enables Discovery of Embedded Bacterial Ferredoxin Domains in Large Redox Enzymes.Proteins · 2025Article
- Deciphering enzymatic potential in metagenomic reads through DNA language models.Nucleic acids research · 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
- Molecular aspects of heat stress sensing in land plants.The Plant journal : for cell and molecular biology · 2025Review
- Article
- BioIron: Origin, Chemical Properties, and Biological Functions.Advances in experimental medicine and biology · 2025Review
- Deep generative models of protein structure uncover distant relationships across a continuous fold space.Nature communications · 2024Article
- Back in time to the Gly-rich prototype of the phosphate binding elementary function.Current research in structural biology · 2024Review
- Coordination chemistry of mitochondrial copper metalloenzymes: exploring implications for copper dyshomeostasis in cell death.BMB reports · 2023Review
- Hunting down zinc(II)-binding sites in proteins with distance matrices.Bioinformatics (Oxford, England) · 2023Article
- Learning from the unknown: exploring the range of bacterial functionality.Nucleic acids research · 2023Article
- Learning in ensembles of proteinoid microspheres.Royal Society open science · 2023Article
- Tracing the birth of structural domains from loops during protein evolution.Scientific reports · 2023Article
- Metals in Prebiotic Catalysis: A Possible Evolutionary Pathway for the Emergence of Metalloproteins.ACS omega · 2023Review
- A self-sustaining serpentinization mega-engine feeds the fougerite nanoengines implicated in the emergence of guided metabolism.Frontiers in microbiology · 2023Article
- Oxytocin and oxygen: the evolution of a solution to the 'stress of life'.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological redox reactions drive planetary biogeochemical cycles. Using a novel, structure-guided sequence analysis of proteins, we explored the patterns of evolution of enzymes responsible for these reactions. Our analysis reveals that the folds that bind transition metal–containing ligands have similar structural geometry and amino acid sequences across the full diversity of proteins. Similarity across folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal–ligand binding had a small number of common peptide origins. We observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions. Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.Thus, life is a special, very complex form of motion of matter, but this form did not always exist, and it is not separated from inorganic nature by an impassable abyss; rather, it arose from inorganic nature as a new property in the process of evolution of the world. We must study the history of this evolution if we want to solve the problem of the origin of life. [A. I. Oparin (
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