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 little is known about electric-field effects on protein function. Here we use phototriggered charge injection from a site-specifically attached ruthenium photosensitizer to directly demonstrate the effects of charge redistribution within a protein. We find that binding of an antibody to phosphoglycerate kinase (PGK) is increased two folds 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
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license. S.G. and K.B.-G. contributed equally to this work. 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 and from the Israel Ministry of Science and Technology. Work at Caltech was supported by the United States NIH (R01 DK019038 to H.B.G.). Author Contributions: S.G. and K.B.-G. designed the project, performed all experiments and analyzed the results, D.L. prepared labeled proteins, D.S. instructed and participated in enzyme kinetics experiments, J.S. and H.B.G provided materials, G.H. and R.N. conceived and supervised the research and wrote the paper with help from all authors. The authors have declared no competing interest.Attached Files
Submitted - 2021.10.12.464058v2.full.pdf
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Additional details
- Eprint ID
- 115692
- DOI
- 10.1101/2021.10.12.464058
- Resolver ID
- CaltechAUTHORS:20220720-917086000
- European Research Council (ERC)
- 742637
- Israel Science Foundation
- 1250/19
- Weizmann SABRA - Yeda-Sela – WRC program
- Hilda Pomeraniec Memorial Professorial Chair
- MINERVA (Israel)
- Ministry of Science and Technology (Israel)
- NIH
- R01 DK019038
- Created
-
2022-07-22Created from EPrint's datestamp field
- Updated
-
2023-03-22Created from EPrint's last_modified field