Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins
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| Main Authors: | , , , , , , , |
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| Format: | Preprint |
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2023
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| _version_ | 1866914984902000640 |
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| author | Lamichhane, Suvechhya Timalsina, Rupak Schultz, Cody Fescenko, Ilja Ambal, Kapildeb Liou, Sy-Hwang Lai, Rebecca Y. Laraoui, Abdelghani |
| author_facet | Lamichhane, Suvechhya Timalsina, Rupak Schultz, Cody Fescenko, Ilja Ambal, Kapildeb Liou, Sy-Hwang Lai, Rebecca Y. Laraoui, Abdelghani |
| contents | 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 Fe3+ state, which is paramagnetic. We vary the concentration of Cyt-C from 6 to 54 uM and observe a reduction of the NV spin-lattice relaxation time (T1) from 1.2 ms to 150 us, which is attributed to the spin noise originating from the Fe3+ spins. NV T1 imaging of Cyt-C drop-casted on a nanostructured diamond chip allows us to detect the relaxation rates from the adsorbed Fe3+ within Cyt-C. |
| format | Preprint |
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arxiv_https___arxiv_org_abs_2310_08605 |
| institution | arXiv |
| publishDate | 2023 |
| record_format | arxiv |
| spellingShingle | Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins Lamichhane, Suvechhya Timalsina, Rupak Schultz, Cody Fescenko, Ilja Ambal, Kapildeb Liou, Sy-Hwang Lai, Rebecca Y. Laraoui, Abdelghani Biological Physics Quantum Physics 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 Fe3+ state, which is paramagnetic. We vary the concentration of Cyt-C from 6 to 54 uM and observe a reduction of the NV spin-lattice relaxation time (T1) from 1.2 ms to 150 us, which is attributed to the spin noise originating from the Fe3+ spins. NV T1 imaging of Cyt-C drop-casted on a nanostructured diamond chip allows us to detect the relaxation rates from the adsorbed Fe3+ within Cyt-C. |
| title | Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins |
| topic | Biological Physics Quantum Physics |
| url | https://arxiv.org/abs/2310.08605 |