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Title: 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 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. In conclusion, 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.
Authors:
ORCiD logo [1] ; ORCiD logo [1] ; ORCiD logo [1] ; ORCiD logo [1] ; ORCiD logo [2] ; ORCiD logo [2] ; ORCiD logo [2] ;  [3] ; ORCiD logo [3] ; ORCiD logo [4] ; ORCiD logo [4] ; ORCiD logo [2] ; ORCiD logo [1] ; ORCiD logo [1]
  1. Univ. of Pennsylvania, Philadelphia, PA (United States). Johnson Research Foundation and Dept. of Biochemistry and Biophysics
  2. Univ. of Wollongong, NSW (Australia). ARC Centre of Excellence for Electromaterials Science and the Intelligent Polymer Research Inst.
  3. North Carolina State Univ., Raleigh, NC (United States). Dept. of Chemistry
  4. Univ. of Otago, Dunedin (New Zealand). Dept. of Chemistry
Publication Date:
Grant/Contract Number:
SC0001035; EB018464
Type:
Accepted Manuscript
Journal Name:
Chemical Science
Additional Journal Information:
Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2041-6520
Publisher:
Royal Society of Chemistry
Research Org:
Washington Univ., St. Louis, MO (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); National Institutes of Health (NIH)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
OSTI Identifier:
1425208

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, and Moser, Christopher C.. Design and engineering of water-soluble light-harvesting protein maquettes. United States: N. p., Web. doi:10.1039/c6sc02417c.
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. United States. doi:10.1039/c6sc02417c.
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, and Moser, Christopher C.. 2017. "Design and engineering of water-soluble light-harvesting protein maquettes". United States. doi:10.1039/c6sc02417c. https://www.osti.gov/servlets/purl/1425208.
@article{osti_1425208,
title = {Design and engineering of water-soluble light-harvesting protein maquettes},
author = {Kodali, Goutham and Mancini, Joshua A. and Solomon, Lee A. and Episova, Tatiana V. and Roach, Nicholas and Hobbs, Christopher J. and Wagner, Pawel and Mass, Olga A. and Aravindu, Kunche and Barnsley, Jonathan E. and Gordon, Keith C. and Officer, David L. and Dutton, P. Leslie and Moser, Christopher C.},
abstractNote = {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. In conclusion, 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.},
doi = {10.1039/c6sc02417c},
journal = {Chemical Science},
number = 1,
volume = 8,
place = {United States},
year = {2017},
month = {1}
}

Works referenced in this record:

Characterization of a helical protein designed from first principles
journal, August 1988

Design and synthesis of multi-haem proteins
journal, March 1994
  • Robertson, Dan E.; Farid, Ramy S.; Moser, Christopher C.
  • Nature, Vol. 368, Issue 6470, p. 425-432
  • DOI: 10.1038/368425a0