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

doi:10.1002/prot.26563

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

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

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.

Original language	English (US)
Pages (from-to)	52-59
Number of pages	8
Journal	Proteins: Structure, Function and Bioinformatics
Volume	92
Issue number	1
DOIs	https://doi.org/10.1002/prot.26563
State	Published - Jan 2024
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Molecular Biology

Keywords

electrons
energy metabolism
enzymes and coenzymes oxidation–reduction oxidoreductases proteins

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10.1002/prot.26563

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McGuinness, K. N., Fehon, N., Feehan, R., Miller, M., Mutter, A. C., Rybak, L. A., Nam, J., AbuSalim, J. E., Atkinson, J. T., Heidari, H., Losada, N., Kim, J. D., Koder, R. L., Lu, Y., Silberg, J. J., Slusky, J. S. G., Falkowski, P. G., & Nanda, V. (2024). The energetics and evolution of oxidoreductases in deep time. Proteins: Structure, Function and Bioinformatics, 92(1), 52-59. https://doi.org/10.1002/prot.26563

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title = "The energetics and evolution of oxidoreductases in deep time",

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 = "electrons, energy metabolism, enzymes and coenzymes oxidation–reduction oxidoreductases proteins",

author = "McGuinness, {Kenneth N.} and Nolan Fehon and Ryan Feehan and Michelle Miller and Mutter, {Andrew C.} and Rybak, {Laryssa A.} and Justin Nam and AbuSalim, {Jenna E.} and Atkinson, {Joshua T.} and Hirbod Heidari and Natalie Losada and Kim, {J. Dongun} and Koder, {Ronald L.} and Yi Lu and Silberg, {Jonathan J.} and Slusky, {Joanna S.G.} and Falkowski, {Paul G.} and Vikas Nanda",

note = "Publisher Copyright: {\textcopyright} 2023 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC.",

year = "2024",

month = jan,

doi = "10.1002/prot.26563",

language = "English (US)",

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McGuinness, KN, Fehon, N, Feehan, R, Miller, M, Mutter, AC, Rybak, LA, Nam, J, AbuSalim, JE, Atkinson, JT, Heidari, H, Losada, N, Kim, JD, Koder, RL, Lu, Y, Silberg, JJ, Slusky, JSG, Falkowski, PG & Nanda, V 2024, 'The energetics and evolution of oxidoreductases in deep time', Proteins: Structure, Function and Bioinformatics, vol. 92, no. 1, pp. 52-59. https://doi.org/10.1002/prot.26563

TY - JOUR

T1 - The energetics and evolution of oxidoreductases in deep time

AU - McGuinness, Kenneth N.

AU - Fehon, Nolan

AU - Feehan, Ryan

AU - Miller, Michelle

AU - Mutter, Andrew C.

AU - Rybak, Laryssa A.

AU - Nam, Justin

AU - AbuSalim, Jenna E.

AU - Atkinson, Joshua T.

AU - Heidari, Hirbod

AU - Losada, Natalie

AU - Kim, J. Dongun

AU - Koder, Ronald L.

AU - Lu, Yi

AU - Silberg, Jonathan J.

AU - Slusky, Joanna S.G.

AU - Falkowski, Paul G.

AU - Nanda, Vikas

PY - 2024/1

Y1 - 2024/1

N2 - 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.

AB - 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.

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ER -

The energetics and evolution of oxidoreductases in deep time

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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