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The energetics and evolution of oxidoreductases in deep time
  • +14
  • Vikas Nanda,
  • Kenneth N. McGuinness,
  • Nolan Fehon,
  • Ryan Feehan,
  • Michelle Miller,
  • Andrew Mutter,
  • Justin Nam,
  • Jenna E. AbuSalim,
  • Joshua T. Atkinson,
  • Hirbod Heidari,
  • Natalie Losada,
  • J. Dongun Kim,
  • Ronald L. Koder,
  • Yi Lu,
  • Joff Silberg,
  • Joanna Slusky,
  • Paul Falkowski
Vikas Nanda
Center for Advanced Biotechnology and Medicine
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Kenneth N. McGuinness
Caldwell University

Corresponding Author:[email protected]

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Nolan Fehon
Rutgers University Institute of Marine and Coastal Sciences
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Ryan Feehan
The University of Kansas
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Michelle Miller
Rutgers University Institute of Marine and Coastal Sciences
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Andrew Mutter
The City College of New York Department of Physics
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Justin Nam
Center for Advanced Biotechnology and Medicine
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Jenna E. AbuSalim
Center for Advanced Biotechnology and Medicine
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Joshua T. Atkinson
Rice University
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Hirbod Heidari
The University of Texas at Austin Department of Chemistry
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Natalie Losada
Center for Advanced Biotechnology and Medicine
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J. Dongun Kim
Rutgers University Institute of Marine and Coastal Sciences
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Ronald L. Koder
The City College of New York Department of Physics
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Yi Lu
The University of Texas at Austin Department of Chemistry
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Joff Silberg
Rice University
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Joanna Slusky
The University of Kansas
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Paul Falkowski
Rutgers University Institute of Marine and Coastal Sciences
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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.
17 May 2023Submitted to PROTEINS: Structure, Function, and Bioinformatics
18 May 2023Review(s) Completed, Editorial Evaluation Pending
18 May 2023Submission Checks Completed
18 May 2023Assigned to Editor
22 May 2023Reviewer(s) Assigned
06 Jul 2023Editorial Decision: Accept