Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins.

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 Fe3+ 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 (T1) from 1.2 ms to 150 µs, 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.