Unveiling the role of inorganic nanoparticles in Earth's biochemical evolution through electron transfer dynamics

Abstract

This article explores the intricate interplay between inorganic nanoparticles and Earth's biochemical history, with a focus on their electron transfer properties. It reveals how iron oxide and sulfide nanoparticles, as examples of inorganic nanoparticles, exhibit oxidoreductase activity similar to proteins. Termed "life fossil oxidoreductases," these inorganic enzymes influence redox reactions, detoxification processes, and nutrient cycling in early Earth environments. By emphasizing the structural configuration of nanoparticles and their electron conformation, including oxygen defects and metal vacancies, especially electron hopping, the article provides a foundation for understanding inorganic enzyme mechanisms. This approach, rooted in physics, underscores that life's origin and evolution are governed by electron transfer principles within the framework of chemical equilibrium. Today, these nanoparticles serve as vital biocatalysts in natural ecosystems, participating in critical reactions for ecosystem health. The research highlights their enduring impact on Earth's history, shaping ecosystems and interacting with protein metal centers through shared electron transfer dynamics, offering insights into early life processes and adaptations.

Keywords: biochemistry; chemistry; inorganic chemistry.

Graphical abstract

Figure 1

Electron Transfer Modes of the Inorganic Oxidoreductase (A) Electron Hopping in Inorganic Nanomaterials (Adopted from electron hopping behavior from iron oxide nanoparticles, reprinting from Katz J E et al., copyright@2012, The American Association for the Advancement of Science), Multiples reports support this observation (green rust, magnetite, iron oxyhydroxides,^,, hematite,^,,, γ-Fe₂O₃; FeS₂,^,,,,, Iron polysulfides (e.g., Fe_1-xS),^,, V₂O₅, Mn₃O₄, MnO₂,^, Co₃O₄,^,, TiO₂,^,, CeO₂,^, α-FeSe, MnSe, and MoSe₂²⁹⁸). (B) Photoelectron Effect and Photothermal Effect. Multiple reports support this observation.^{,,,,,,,,,,,,,,,} (C) Electron mediation by Cytochrome c (Adopted from Direct Electron Transfer of Enzymes Facilitated by Cytochromes and reprinting from Ma and Ludwing⁸⁷) Multiple reports support this observation.^,,,,,,,