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Design and engineering of water-soluble light-harvesting protein maquettes

Natural selection in photosynthesis has engineered tetrapyrrole based, nanometer scale, light harvesting and energy capture in light-induced charge separation. By designing and creating nanometer scale artificial light harvesting and charge separating proteins, we have the opportunity to reengineer...

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Autores principales: Kodali, Goutham, Mancini, Joshua A., Solomon, Lee A., Episova, Tatiana V., Roach, Nicholas, Hobbs, Christopher J., Wagner, Pawel, Mass, Olga A., Aravindu, Kunche, Barnsley, Jonathan E., Gordon, Keith C., Officer, David L., Dutton, P. Leslie, Moser, Christopher C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5330312/
https://www.ncbi.nlm.nih.gov/pubmed/28261441
http://dx.doi.org/10.1039/c6sc02417c
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author Kodali, Goutham
Mancini, Joshua A.
Solomon, Lee A.
Episova, Tatiana V.
Roach, Nicholas
Hobbs, Christopher J.
Wagner, Pawel
Mass, Olga A.
Aravindu, Kunche
Barnsley, Jonathan E.
Gordon, Keith C.
Officer, David L.
Dutton, P. Leslie
Moser, Christopher C.
author_facet Kodali, Goutham
Mancini, Joshua A.
Solomon, Lee A.
Episova, Tatiana V.
Roach, Nicholas
Hobbs, Christopher J.
Wagner, Pawel
Mass, Olga A.
Aravindu, Kunche
Barnsley, Jonathan E.
Gordon, Keith C.
Officer, David L.
Dutton, P. Leslie
Moser, Christopher C.
author_sort Kodali, Goutham
collection PubMed
description Natural selection in photosynthesis has engineered tetrapyrrole based, nanometer scale, light harvesting and energy capture in light-induced charge separation. By designing and creating nanometer scale artificial light harvesting and charge separating proteins, we have the opportunity to reengineer and overcome the limitations of natural selection to extend energy capture to new wavelengths and to tailor efficient systems that better meet human as opposed to cellular energetic needs. While tetrapyrrole cofactor incorporation in natural proteins is complex and often assisted by accessory proteins for cofactor transport and insertion, artificial protein functionalization relies on a practical understanding of the basic physical chemistry of protein and cofactors that drive nanometer scale self-assembly. Patterning and balancing of hydrophobic and hydrophilic tetrapyrrole substituents is critical to avoid natural or synthetic porphyrin and chlorin aggregation in aqueous media and speed cofactor partitioning into the non-polar core of a man-made water soluble protein designed according to elementary first principles of protein folding. This partitioning is followed by site-specific anchoring of tetrapyrroles to histidine ligands strategically placed for design control of rates and efficiencies of light energy and electron transfer while orienting at least one polar group towards the aqueous phase.
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spelling pubmed-53303122017-04-27 Design and engineering of water-soluble light-harvesting protein maquettes Kodali, Goutham Mancini, Joshua A. Solomon, Lee A. Episova, Tatiana V. Roach, Nicholas Hobbs, Christopher J. Wagner, Pawel Mass, Olga A. Aravindu, Kunche Barnsley, Jonathan E. Gordon, Keith C. Officer, David L. Dutton, P. Leslie Moser, Christopher C. Chem Sci Chemistry Natural selection in photosynthesis has engineered tetrapyrrole based, nanometer scale, light harvesting and energy capture in light-induced charge separation. By designing and creating nanometer scale artificial light harvesting and charge separating proteins, we have the opportunity to reengineer and overcome the limitations of natural selection to extend energy capture to new wavelengths and to tailor efficient systems that better meet human as opposed to cellular energetic needs. While tetrapyrrole cofactor incorporation in natural proteins is complex and often assisted by accessory proteins for cofactor transport and insertion, artificial protein functionalization relies on a practical understanding of the basic physical chemistry of protein and cofactors that drive nanometer scale self-assembly. Patterning and balancing of hydrophobic and hydrophilic tetrapyrrole substituents is critical to avoid natural or synthetic porphyrin and chlorin aggregation in aqueous media and speed cofactor partitioning into the non-polar core of a man-made water soluble protein designed according to elementary first principles of protein folding. This partitioning is followed by site-specific anchoring of tetrapyrroles to histidine ligands strategically placed for design control of rates and efficiencies of light energy and electron transfer while orienting at least one polar group towards the aqueous phase. Royal Society of Chemistry 2017-01-01 2016-08-17 /pmc/articles/PMC5330312/ /pubmed/28261441 http://dx.doi.org/10.1039/c6sc02417c Text en This journal is © The Royal Society of Chemistry 2016 http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Kodali, Goutham
Mancini, Joshua A.
Solomon, Lee A.
Episova, Tatiana V.
Roach, Nicholas
Hobbs, Christopher J.
Wagner, Pawel
Mass, Olga A.
Aravindu, Kunche
Barnsley, Jonathan E.
Gordon, Keith C.
Officer, David L.
Dutton, P. Leslie
Moser, Christopher C.
Design and engineering of water-soluble light-harvesting protein maquettes
title Design and engineering of water-soluble light-harvesting protein maquettes
title_full Design and engineering of water-soluble light-harvesting protein maquettes
title_fullStr Design and engineering of water-soluble light-harvesting protein maquettes
title_full_unstemmed Design and engineering of water-soluble light-harvesting protein maquettes
title_short Design and engineering of water-soluble light-harvesting protein maquettes
title_sort design and engineering of water-soluble light-harvesting protein maquettes
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5330312/
https://www.ncbi.nlm.nih.gov/pubmed/28261441
http://dx.doi.org/10.1039/c6sc02417c
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