Issue 5, 2026

Interactions of early actinides with biologically-relevant organic molecules including carboxylates, amino acids and proteins

Abstract

This Perspective article reviews the current knowledge regarding the interaction of actinide elements with biomolecules, particularly amino acids, peptides, and proteins. We assess the significance of these interactions, especially in connection to nuclear waste disposal and the potential role of these interactions in the origin of life. Actinides have been observed to form stable complexes with carboxylate groups, resulting in oligomerization and affecting their environmental mobility. The text discusses the complex coordination chemistry of actinides, including the prevalence of hexanuclear An4+ clusters, and the implications of these findings for actinide transport and bioavailability as well as remaining challenges especially for mechanistic and thermodynamic aspects of this chemistry. Recent discoveries of lanthanide- and actinide-dependent enzymes, including methanol dehydrogenase and lanmodulin, suggest a potential for these elements to have been actively involved in early metabolic processes, rather than solely acting as environmental stressors. Despite the absence of direct evidence connecting natural reactors to the process of abiogenesis, a comprehensive understanding of actinide–biomolecule interactions is imperative for the evaluation of the nuclear geyser model and the resolution of the long-term challenges posed by the management of radioactive waste.

Graphical abstract: Interactions of early actinides with biologically-relevant organic molecules including carboxylates, amino acids and proteins

Article information

Article type
Perspective
Submitted
08 Oct 2025
Accepted
22 Dec 2025
First published
02 Jan 2026
This article is Open Access
Creative Commons BY license

Dalton Trans., 2026,55, 1938-1957

Interactions of early actinides with biologically-relevant organic molecules including carboxylates, amino acids and proteins

S. Tsushima and K. Takao, Dalton Trans., 2026, 55, 1938 DOI: 10.1039/D5DT02408K

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