Control of protein activity by photoinduced spin polarized charge reorganization
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.
Additional Information
© 2022 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY). This work was partially supported by a grant to G.H. from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation program (grant agreement No 742637, SMALLOSTERY), a grant from the Israel Science Foundation (no. 1250/19) and a grant from the Weizmann SABRA-Yeda-Sela-WRC program. G.H. holds the Hilda Pomeraniec Memorial Professorial Chair. R.N. acknowledges partial support from the MINERVA Foundation, from the Israel Ministry of Science and Technology, and from the AFOSR (FA9550-21-1-0418). Work at Caltech was supported by the United States NIH (R01 DK019038 to H.B.G.). Data, Materials, and Software Availability. All study data are included in the article and/or supporting information. The authors declare no competing interest.Attached Files
Published - pnas.202204735.pdf
Supplemental Material - pnas.2204735119.sapp.pdf
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Additional details
- PMCID
- PMC9436351
- Eprint ID
- 119198
- Resolver ID
- CaltechAUTHORS:20230210-192713382
- 742637
- European Research Council (ERC)
- 1250/19
- Israel Science Foundation
- Weizmann Institute of Science
- MINERVA (Israel)
- Ministry of Science and Technology (Israel)
- FA9550-21-1-0418
- Air Force Office of Scientific Research (AFOSR)
- DK019038
- NIH
- Created
-
2023-03-22Created from EPrint's datestamp field
- Updated
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2023-07-21Created from EPrint's last_modified field