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), 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.
Keywords: oxidation-reduction; proteins; energy metabolism;
electrons; oxidoreductases, enzymes and coenzymes