ArticlePLoS computational biology2012
Energetic selection of topology in ferredoxins.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Article
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- 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
- Natural selection based on coordination chemistry: computational assessment of [4Fe-4S]-maquettes with non-coded amino acids.Interface focus · 2019Article
- Radical S-adenosylmethionine maquette chemistry: CxJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer.Journal of the American Chemical Society · 2018Article
- Green Rust: The Simple Organizing 'Seed' of All Life?Life (Basel, Switzerland) · 2018Review
- Structural principles for computational and de novo design of 4Fe-4S metalloproteins.Biochimica et biophysica acta · 2016Review
- From Light to Life.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2015Article
- Empirical estimation of local dielectric constants: Toward atomistic design of collagen mimetic peptides.Biopolymers · 2015Article
- Evolutionary history of redox metal-binding domains across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Discovering the electronic circuit diagram of life: structural relationships among transition metal binding sites in oxidoreductases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Anoxic photochemical oxidation of siderite generates molecular hydrogen and iron oxides.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Models of early protein evolution posit the existence of short peptides that bound metals and ions and served as transporters, membranes or catalysts. The Cys-X-X-Cys-X-X-Cys heptapeptide located within bacterial ferredoxins, enclosing an Fe₄S₄ metal center, is an attractive candidate for such an early peptide. Ferredoxins are ancient proteins and the simple α+β fold is found alone or as a domain in larger proteins throughout all three kingdoms of life. Previous analyses of the heptapeptide conformation in experimentally determined ferredoxin structures revealed a pervasive right-handed topology, despite the fact that the Fe₄S₄ cluster is achiral. Conformational enumeration of a model CGGCGGC heptapeptide bound to a cubane iron-sulfur cluster indicates both left-handed and right-handed folds could exist and have comparable stabilities. However, only the natural ferredoxin topology provides a significant network of backbone-to-cluster hydrogen bonds that would stabilize the metal-peptide complex. The optimal peptide configuration (alternating α(L),α(R)) is that of an α-sheet, providing an additional mechanism where oligomerization could stabilize the peptide and facilitate iron-sulfur cluster binding.
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