All-Optical Spin Coherence in a Photosynthetic Electron-Transfer Metalloprotein
- 1Arthur Amos Noyes Laboratory of Chemical Physics
- 2California Institute of Technology
Abstract
Optically addressable, biocompatible spin qubits represent promising platforms for quantum sensing. However, current efforts have focused on genetic encodability and microwave-based approaches thus far limited to organic radicals. Utilizing time-resolved Faraday rotation, we measured electron spin coherence in plastocyanin, a protein in the photosynthetic electron transport chain. Persisting hundreds of picoseconds, this is the first measurement of spin coherence in a metalloprotein under ambient conditions. We show how the protein’s active-site geometric and electronic structure responsible for biological function also enabled a spin–photon interface. A related blue copper protein—azurin—also demonstrated all-optical spin coherence. The ability to measure bioinorganic spin coherence under functional conditions foreshadows metalloproteins as native quantum sensors and opens questions about the potential role of spin coherences in electron transfer.
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BibTeX
@misc{totoiu2026alloptical,
title = {{All-Optical Spin Coherence in a Photosynthetic Electron-Transfer Metalloprotein}},
author = {Christian A. Totoiu and Erica Sutcliffe and Demetrios A. Dresios and Ryan G. Hadt},
howpublished = {ChemRxiv},
year = {2026},
month = oct,
doi = {10.26434/chemrxiv.15009712/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009712/v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - All-Optical Spin Coherence in a Photosynthetic Electron-Transfer Metalloprotein
AU - Christian A. Totoiu
AU - Erica Sutcliffe
AU - Demetrios A. Dresios
AU - Ryan G. Hadt
PY - 2026
DA - 2026/10/01
PB - ChemRxiv
DO - 10.26434/chemrxiv.15009712/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009712/v1
AB - Optically addressable, biocompatible spin qubits represent promising platforms for quantum sensing. However, current efforts have focused on genetic encodability and microwave-based approaches thus far limited to organic radicals. Utilizing time-resolved Faraday rotation, we measured electron spin coherence in plastocyanin, a protein in the photosynthetic electron transport chain. Persisting hundreds of picoseconds, this is the first measurement of spin coherence in a metalloprotein under ambient conditions. We show how the protein’s active-site geometric and electronic structure responsible for biological function also enabled a spin–photon interface. A related blue copper protein—azurin—also demonstrated all-optical spin coherence. The ability to measure bioinorganic spin coherence under functional conditions foreshadows metalloproteins as native quantum sensors and opens questions about the potential role of spin coherences in electron transfer.
ER -