Quantification of redox thermodynamics shifts within coacervates.

ABSTRACT: Coacervates are suggested to be viable protoenzymes due to their propensity to act as catalytic microreactors for biochemical reactions. However, the mechanism by which they alter reaction thermodynamics remains unclear. While extensive research has been conducted displaying the ability of coacervates to compartmentalize a wide variety of reactants, products, and catalysts, insight into how reactant, transition state, and product energies are altered within the droplet continues to be an active area of research. One promising strategy for investigating the thermodynamics and kinetics within the coacervate phase is temperature-dependent electrochemistry, which enables the extraction of reaction entropy, enthalpy, and Gibbs energy. In this work, we use ferri/ferrocyanide, a well-behaved redo

SUBMITTER: Rodriguez G 

PROVIDER: S-EPMC12646308 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature