Control of protein activity by photoinduced spin polarized charge reorganization

Ghosh, Shirsendu and Ghosh, Koyel Banerjee and Levy, Dorit and et al, . (2022) Control of protein activity by photoinduced spin polarized charge reorganization. Proceedings of the National Academy of Sciences, 119 (35). pp. 1-6. ISSN 0027-8424

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Abstract

Considerable electric fields are present within living cells, and the role of bioelectricity has been well established at the organismal level. Yet much remains to be learned about electric-field effects on protein function. Here, we use phototriggered charge injection from a site-specifically attached ruthenium photosensitizer to directly demonstrate the effect of dynamic charge redistribution within a protein. We find that binding of an antibody to phosphoglycerate kinase (PGK) is increased twofold under illumination. Remarkably, illumination is found to suppress the enzymatic activity of PGK by a factor as large as three. These responses are sensitive to the photosensitizer position on the protein. Surprisingly, left (but not right) circularly polarized light elicits these responses, indicating that the electrons involved in the observed dynamics are spin polarized, due to spin filtration by protein chiral structures. Our results directly establish the contribution of electrical polarization as an allosteric signal within proteins. Future experiments with phototriggered charge injection will allow delineation of charge rearrangement pathways within proteins and will further depict their effects on protein function.

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IITH Creators:
IITH CreatorsORCiD
Ghosh, Koyel BanerjeeUNSPECIFIED
Item Type: Article
Uncontrolled Keywords: allostery; chiral-induced spin selectivity; enzymatic activity; polarizability; protein-protein association
Subjects: Chemistry
Divisions: Department of Chemistry
Depositing User: . LibTrainee 2021
Date Deposited: 01 Sep 2022 09:54
Last Modified: 01 Sep 2022 09:54
URI: http://raiithold.iith.ac.in/id/eprint/10378
Publisher URL: http://doi.org/10.1073/pnas.2204735119
OA policy: https://v2.sherpa.ac.uk/id/publication/10338
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