Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer

Bromberg, Yana; Aptekmann, Ariel; Mahlich, Yannick; Cook, L. F.; Senn, Stefan; Miller, Maximillian; Nanda, Vikas; Ferreiro, Diego U.; Falkowski, Paul G.

doi:10.1126/sciadv.abj3984

Cited by 35 publications

(41 citation statements)

References 78 publications

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“… ‘… 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.’ [ 1 , p.1] …”

Section: Overviewmentioning

confidence: 99%

“…During that period biological systems gradually emerged capable of the management of gases (including oxygen), fluids (including water), nutrients (carbohydrates, fats, amino acids and minerals) and various mechanisms for the defence of tissues and organisms (including cytokines and immune systems). The origins and mechanisms for the diverse interactions between oxygen and the precursors for OT go back to the point at which peptides first became involved in the origins of life, estimated at approximately 3.8 billion years ago (Ba) [ 1 ]. Peptide molecules including OT-like molecules were early components of cellular defences and homeostatic mechanisms, with subsequent consequences for vertebrate development and behaviour, and the management of challenges and stressors [ 1 , 5 ].…”

Section: Originsmentioning

confidence: 99%

“…The origins and mechanisms for the diverse interactions between oxygen and the precursors for OT go back to the point at which peptides first became involved in the origins of life, estimated at approximately 3.8 billion years ago (Ba) [ 1 ]. Peptide molecules including OT-like molecules were early components of cellular defences and homeostatic mechanisms, with subsequent consequences for vertebrate development and behaviour, and the management of challenges and stressors [ 1 , 5 ].…”

Section: Originsmentioning

confidence: 99%

“…Peptide molecules are integrated into all aspects of life. Peptides allowed living organisms to use elements including oxygen, carbon, nitrogen, hydrogen, sulfur and various metals to create amino acids [ 1 ]. They also supported growth, adaptation, protection and reproduction .…”

Section: The Evolved Power Of Peptidesmentioning

confidence: 99%

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Oxytocin and oxygen: the evolution of a solution to the ‘stress of life’

Carter

Kingsbury

2022

Phil. Trans. R. Soc. B

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Oxytocin (OT) and the OT receptor occupy essential roles in our current understanding of mammalian evolution, survival, sociality and reproduction. This narrative review examines the hypothesis that many functions attributed to OT can be traced back to conditions on early Earth, including challenges associated with managing life in the presence of oxygen and other basic elements, including sulfur. OT regulates oxidative stress and inflammation especially through effects on the mitochondria. A related nonapeptide, vasopressin, as well as molecules in the hypothalamic–pituitary–adrenal axis, including the corticotropin-releasing hormone family of molecules, have a broad set of functions that interact with OT. Interactions among these molecules have roles in the causes and consequence of social behaviour and the management of threat, fear and stress. Here, we discuss emerging evidence suggesting that unique properties of the OT system allowed vertebrates, and especially mammals, to manage over-reactivity to the ‘side effects’ of oxygen, including inflammation, oxidation and free radicals, while also supporting high levels of sociality and a perception of safety. This article is part of the theme issue ‘Interplays between oxytocin and other neuromodulators in shaping complex social behaviours’.

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Section: Overviewmentioning

confidence: 99%

Section: Originsmentioning

confidence: 99%

Section: Originsmentioning

confidence: 99%

Section: The Evolved Power Of Peptidesmentioning

confidence: 99%

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Oxytocin and oxygen: the evolution of a solution to the ‘stress of life’

Carter

Kingsbury

2022

Phil. Trans. R. Soc. B

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“…Even more, though big steps are being made in this direction [2], since these systems have been developing over a billion of years of evolution, this kind of analysis is constrained by the time at which the networks are sampled, limiting insight into their evolutionary history. Efforts are also being done to overcome this time constraint, such as inferring ancestral metabolic networks using methods to estimate the genetic distance between different bacterial species as given by phylogenetic trees built following the maximum parsimony criterion [3], and also using structure-guided sequence analysis of proteins to explore the patterns of evolution of enzymes responsible for biogeochemical cycles [4].…”

Section: Introductionmentioning

confidence: 99%

Evolutionary timeline of a modeled cell

Ibarra-Junquera¹,

Radillo-Ochoa²,

Terrero-Escalante³

2022

Preprint

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A theoretical study of cell evolution is presented here. By using a toolbox containing an intracellular catalytic reaction network model and a mutation-selection process, four distinct phases of self-organization were unveiled. First, the nutrients prevail as the central substrate of the chemical reactions. Second, the cell becomes a small-world. Third, a highly connected core component emerges, concurrently with the nutrient carriers becoming the central product of reactions. Finally, the cell reaches a steady configuration where the concentrations of the core chemical species are described by Zipf's law.

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Histidine Ligated Iron‐Sulfur Peptides

et al. 2022

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Iron‐sulfur clusters are thought to be ancient cofactors that could have played a role in early protometabolic systems. Thus far, redox active, prebiotically plausible iron‐sulfur clusters have always contained cysteine ligands to the cluster. However, extant iron‐sulfur proteins can be found to exploit other modes of binding, including ligation by histidine residues, as seen with [2Fe‐2S] Rieske and MitoNEET proteins. Here, we investigated the ability of cysteine‐ and histidine‐containing peptides to coordinate a mononuclear Fe2+ center and a [2Fe‐2S] cluster and compare their properties with purified iron‐sulfur proteins. The iron‐sulfur peptides were characterized by UV‐vis, circular dichroism, and paramagnetic NMR spectroscopies and cyclic voltammetry. Small (≤6 amino acids) peptides can coordinate [2Fe‐2S] clusters through a combination of cysteine and histidine residues with similar reduction potentials as their corresponding proteins. Such complexes may have been important for early cell‐like systems.

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Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer

Abstract: Computational exploration of similarities among metal-binding protein structural motifs elucidates the origins of life.

Cited by 35 publications

References 78 publications

Oxytocin and oxygen: the evolution of a solution to the ‘stress of life’

Oxytocin and oxygen: the evolution of a solution to the ‘stress of life’

Evolutionary timeline of a modeled cell

Histidine Ligated Iron‐Sulfur Peptides

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