ArticleProceedings of the National Academy of Sciences of the United States of America2018
Modular origins of biological electron transfer chains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Article
- A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.Nature structural & molecular biology · 2025Article
- 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
- BioIron: Origin, Chemical Properties, and Biological Functions.Advances in experimental medicine and biology · 2025Review
- Reused Protein Segments Linked to Functional Dynamics.Molecular biology and evolution · 2024Article
- A concept for international societally relevant microbiology education and microbiology knowledge promulgation in society.Microbial biotechnology · 2024Article
- Article
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Designed Rubredoxin miniature in a fully artificial electron chain triggered by visible light.Nature communications · 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
- Structural Bioinformatics and Deep Learning of Metalloproteins: Recent Advances and Applications.International journal of molecular sciences · 2022Review
- Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Small protein folds at the root of an ancient metabolic network.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals.Life (Basel, Switzerland) · 2019Article
- Evolutionary Relationships Between Low Potential Ferredoxin and Flavodoxin Electron Carriers.Frontiers in energy research · 2019Article
- Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer.Journal of the American Chemical Society · 2018Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oxidoreductases catalyze electron transfer reactions that ultimately provide the energy for life. A limited set of ancestral protein-metal modules are presumably the building blocks that evolved into this diverse protein family. However, the identity of these modules and their path to modern oxidoreductases is unknown. Using a comparative structural analysis approach, we identify a set of fundamental electron transfer modules that have evolved to form the extant oxidoreductases. Using transition metal-containing cofactors as fiducial markers, it is possible to cluster cofactor microenvironments into as few as four major modules: bacterial ferredoxin, cytochrome c, symerythrin, and plastocyanin-type folds. From structural alignments, it is challenging to ascertain whether modules evolved from a single common ancestor (homology) or arose by independent convergence on a limited set of structural forms (analogy). Additional insight into common origins is contained in the spatial adjacency network (SPAN), which is based on proximity of modules in oxidoreductases containing multiple cofactor electron transfer chains. Electron transfer chains within complex modern oxidoreductases likely evolved through repeated duplication and diversification of ancient modular units that arose in the Archean eon.
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