Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins

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Authors
Lamichhane, Suvechhya
Timalsina, Rupak
Schultz, Cody
Fescenko, Ilja
Ambal, Kapildeb
Liou, Sy-Hwang
Lai, Rebecca Y.
Laraoui, Abdelghani
Advisors
Issue Date
2024-01
Type
Article
Keywords
Carbon , Electron paramagnetic resonance spectroscopy , Lasers , Nanoclusters , Quantum mechanics
Research Projects
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Citation
Lamichhane, S., Timalsina, R., Schultz, C., Fescenko, I., Ambal, K., Liou, S., Lai, R.Y., & Laraoui, A. (2024). Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins. Nano Letters. https://doi.org/10.1021/acs.nanolett.3c03843
Abstract

Nitrogen-vacancy (NV) magnetometry offers an alternative tool to detect paramagnetic centers in cells with a favorable combination of magnetic sensitivity and spatial resolution. Here, we employ NV magnetic relaxometry to detect cytochrome C (Cyt-C) nanoclusters. Cyt-C is a water-soluble protein that plays a vital role in the electron transport chain of mitochondria. Under ambient conditions, the heme group in Cyt-C remains in the Fe state, which is paramagnetic. We vary the concentration of Cyt-C from 6 to 54 μM and observe a reduction of the NV spin-lattice relaxation time (T) from 1.2 ms to 150 μs, which is attributed to the spin noise originating from the Fe spins. NV T imaging of Cyt-C drop-casted on a nanostructured diamond chip allows us to detect the relaxation rates from the adsorbed Fe within Cyt-C.

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Publisher
American Chemical Society
Journal
Book Title
Series
Nano Letters
PubMed ID
DOI
ISSN
1530-6984
EISSN