Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin

Scintilla, Simone; Bonfio, Claudia; Belmonte, Luca; Forlin, Michele; Rossetto, Daniele; Li, Jingwei; Cowan, J. A.; Galliani, Angela; Arnesano, Fabio; Assfalg, Michael; Mansy, Sheref S.

doi:10.1039/c6cc07912a

Cited by 39 publications

(54 citation statements)

References 26 publications

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“…Fe 3+ was used instead of Fe 2+ , because the standard protocols for the in vitro maturation of iron-sulfur proteins in aqueous solution utilize ferric salts. Glutathione was used as the model prebiotic thiolate, because this tripeptide (γECG) has previously been shown to coordinate an iron-sulfur cluster13, to function as a protoferredoxin6, and the formation of glutathione was calculated to be thermodynamically favored over the corresponding α-peptide14. Prior to exposure to UV light, the solution of Fe 3+ -glutathione was violet with a UV-visible absorption spectrum similar to that of the mononuclear iron protein rubredoxin (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Iron-sulfur clusters coordinated by cysteine containing peptides are stable to the pH and salt conditions6 needed for the formation of vesicles from fatty acids. Furthermore, the cysteine containing peptides protect the vesicles from the degradative effects of softer, thiophilic metals.…”

Section: Discussionmentioning

confidence: 99%

“…We suggest that a more likely alternative is that short, prebiotically formed peptides helped to assemble and stabilize catalytically active iron-sulfur clusters. Support for this theory comes from the ability of a tripeptide to coordinate a redox active [2Fe-2S] cluster in aqueous solution and that oligomerization of this tripeptide sequence to the dodecapeptide leads to a protoferredoxin with increased cluster stability and activity as a redox catalyst6. The abiological synthesis of iron-sulfur clusters in aqueous solution is typically accomplished by mixing Fe 3+ , S 2– , and suitable thiolate ligands under anaerobic conditions.…”

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confidence: 99%

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UV-light-driven prebiotic synthesis of iron–sulfur clusters

et al. 2017

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Iron-sulfur clusters are ancient cofactors that play a fundamental role in metabolism and may have impacted the prebiotic chemistry that led to life. However, it is unclear whether iron-sulfur clusters could have been synthesized on prebiotic Earth. Dissolved iron on early Earth was predominantly in the reduced ferrous state, but ferrous ions alone cannot form polynuclear iron-sulfur clusters. Similarly, free sulfide may not have been readily available. Here we show that UV light drives the synthesis of [2Fe-2S] and [4Fe-4S] clusters through the photooxidation of ferrous ions and the photolysis of organic thiols. Iron-sulfur clusters coordinate to and are stabilized by a wide range of cysteine-containing peptides and the assembly of iron-sulfur cluster-peptide complexes can take place within model protocells in a process that parallels extant pathways. Our experiments suggest that iron-sulfur clusters may have formed easily on early Earth, facilitating the emergence of an iron-sulfur-cluster-dependent metabolism.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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UV-light-driven prebiotic synthesis of iron–sulfur clusters

et al. 2017

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“…As such, the next step will be to design and study plausible primordial peptides for redox activity. Engineered minimal forms of ferredoxin and Rossmann-like folds are currently being pursued (37,41,48,54), testing the plausibility that modern complex metabolism had its origins in a few ancient peptide oxidoreductases. work.…”

Section: Discussionmentioning

confidence: 99%

Small protein folds at the root of an ancient metabolic network

Raanan

Poudel

Pike

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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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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“…In the prebiotic context, Gazit and coworkers have shown both that aromatic dipeptide assemblies stabilize RNA [19] and that assemblies of phenylalanine and zinc cations exhibit strong hydrolase activity [20]. Mansy and coworkers have investigated the redox activity of short peptide and iron-sulfur cluster nanosized assemblies as a putative origin of ferredoxins [21,22].…”

Section: Introductionmentioning

confidence: 99%

Protoenzymes: The Case of Hyperbranched Polymer-Scaffolded ZnS Nanocrystals

Mamajanov

Caudan

Jia

2020

Life

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Enzymes are biological catalysts that are comprised of small-molecule, metal, or cluster catalysts augmented by biopolymeric scaffolds. It is conceivable that early in chemical evolution, ancestral enzymes opted for simpler, easier to assemble scaffolds. Herein, we describe such possible protoenzymes: hyperbranched polymer-scaffolded metal-sulfide nanocrystals. Hyperbranched polyethyleneimine (HyPEI) and glycerol citrate polymer-supported ZnS nanocrystals (NCs) are formed in a simple process. Transmission electron microscopy (TEM) analyses of HyPEI-supported NCs reveal spherical particles with an average size of 10 nm that undergo only a modest aggregation over a 14-day incubation. The polymer-supported ZnS NCs are shown to possess a high photocatalytic activity in an eosin B photodegradation assay, making them an attractive model for the study of the origin of life under the “Zn world” theory dominated by a photocatalytic proto-metabolic redox reaction network. The catalyst, however, could be easily adapted to apply broadly to different protoenzymatic systems.

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Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin

Cited by 39 publications

References 26 publications

UV-light-driven prebiotic synthesis of iron–sulfur clusters

UV-light-driven prebiotic synthesis of iron–sulfur clusters

Small protein folds at the root of an ancient metabolic network

Protoenzymes: The Case of Hyperbranched Polymer-Scaffolded ZnS Nanocrystals

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