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Rational design of photosynthetic reaction center protein maquettes
New technologies for efficient solar-to-fuel energy conversion will help facilitate a global shift from dependence on fossil fuels to renewable energy. Nature uses photosynthetic reaction centers to convert photon energy into a cascade of electron-transfer reactions that eventually produce chemical...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9532970/ https://www.ncbi.nlm.nih.gov/pubmed/36213121 http://dx.doi.org/10.3389/fmolb.2022.997295 |
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author | Ennist, Nathan M. Stayrook, Steven E. Dutton, P. Leslie Moser, Christopher C. |
author_facet | Ennist, Nathan M. Stayrook, Steven E. Dutton, P. Leslie Moser, Christopher C. |
author_sort | Ennist, Nathan M. |
collection | PubMed |
description | New technologies for efficient solar-to-fuel energy conversion will help facilitate a global shift from dependence on fossil fuels to renewable energy. Nature uses photosynthetic reaction centers to convert photon energy into a cascade of electron-transfer reactions that eventually produce chemical fuel. The design of new reaction centers de novo deepens our understanding of photosynthetic charge separation and may one day allow production of biofuels with higher thermodynamic efficiency than natural photosystems. Recently, we described the multi-step electron-transfer activity of a designed reaction center maquette protein (the RC maquette), which can assemble metal ions, tyrosine, a Zn tetrapyrrole, and heme into an electron-transport chain. Here, we detail our modular strategy for rational protein design and show that the intended RC maquette design agrees with crystal structures in various states of assembly. A flexible, dynamic apo-state collapses by design into a more ordered holo-state upon cofactor binding. Crystal structures illustrate the structural transitions upon binding of different cofactors. Spectroscopic assays demonstrate that the RC maquette binds various electron donors, pigments, and electron acceptors with high affinity. We close with a critique of the present RC maquette design and use electron-tunneling theory to envision a path toward a designed RC with a substantially higher thermodynamic efficiency than natural photosystems. |
format | Online Article Text |
id | pubmed-9532970 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95329702022-10-06 Rational design of photosynthetic reaction center protein maquettes Ennist, Nathan M. Stayrook, Steven E. Dutton, P. Leslie Moser, Christopher C. Front Mol Biosci Molecular Biosciences New technologies for efficient solar-to-fuel energy conversion will help facilitate a global shift from dependence on fossil fuels to renewable energy. Nature uses photosynthetic reaction centers to convert photon energy into a cascade of electron-transfer reactions that eventually produce chemical fuel. The design of new reaction centers de novo deepens our understanding of photosynthetic charge separation and may one day allow production of biofuels with higher thermodynamic efficiency than natural photosystems. Recently, we described the multi-step electron-transfer activity of a designed reaction center maquette protein (the RC maquette), which can assemble metal ions, tyrosine, a Zn tetrapyrrole, and heme into an electron-transport chain. Here, we detail our modular strategy for rational protein design and show that the intended RC maquette design agrees with crystal structures in various states of assembly. A flexible, dynamic apo-state collapses by design into a more ordered holo-state upon cofactor binding. Crystal structures illustrate the structural transitions upon binding of different cofactors. Spectroscopic assays demonstrate that the RC maquette binds various electron donors, pigments, and electron acceptors with high affinity. We close with a critique of the present RC maquette design and use electron-tunneling theory to envision a path toward a designed RC with a substantially higher thermodynamic efficiency than natural photosystems. Frontiers Media S.A. 2022-09-21 /pmc/articles/PMC9532970/ /pubmed/36213121 http://dx.doi.org/10.3389/fmolb.2022.997295 Text en Copyright © 2022 Ennist, Stayrook, Dutton and Moser. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Ennist, Nathan M. Stayrook, Steven E. Dutton, P. Leslie Moser, Christopher C. Rational design of photosynthetic reaction center protein maquettes |
title | Rational design of photosynthetic reaction center protein maquettes |
title_full | Rational design of photosynthetic reaction center protein maquettes |
title_fullStr | Rational design of photosynthetic reaction center protein maquettes |
title_full_unstemmed | Rational design of photosynthetic reaction center protein maquettes |
title_short | Rational design of photosynthetic reaction center protein maquettes |
title_sort | rational design of photosynthetic reaction center protein maquettes |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9532970/ https://www.ncbi.nlm.nih.gov/pubmed/36213121 http://dx.doi.org/10.3389/fmolb.2022.997295 |
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