Abstract
The core metabolic reactions of life drive electrons through a class of
redox protein enzymes, the oxidoreductases. The energetics of electron
flow is determined by the redox potentials of organic and inorganic
cofactors as tuned by the protein environment. Understanding how protein
structure affects oxidation-reduction energetics is crucial for studying
metabolism, creating bioelectronic systems, and tracing the history of
biological energy utilization on Earth. We constructed ProtReDox
([https://protein-redox-potential.web.app](https://protein-redox-potential.web.app)),
a manually curated database of experimentally determined redox
potentials. With over 500 measurements, we can begin to identify how
proteins modulate oxidation-reduction energetics across the tree of
life. By mapping redox potentials onto networks of oxidoreductase fold
evolution, we can infer the evolution of electron transfer energetics
over deep-time. ProtReDox is designed to include user-contributed
submissions with the intention of making it a valuable resource for
researchers in this field.