The energetics and evolution of oxidoreductases in deep time
Kenneth N. McGuinness, Nolan Fehon, Ryan Feehan, Michelle Miller, Andrew C. Mutter, Laryssa A. Rybak, Justin Nam, Jenna E. AbuSalim, Joshua T. Atkinson, Hirbod Heidari, Natalie Losada, J. Dongun Kim, Ronald L. Koder, Yi Lu, Jonathan J. Silberg, Joanna S.G. Slusky, Paul G. Falkowski, Vikas Nanda
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.