Quantum spin dynamics

Abstract:

Coherent control of individual molecular spins in nano-devices is a pivotal prerequisite for fulfilling the potential promised by molecular spintronics. By applying electric field pulses during time-resolved electron spin resonance measurements, we measure the sensitivity of the spin in several antiferromagnetic molecular nanomagnets to external electric fields. We find a linear electric field dependence of the spin states in Cr$_7$Mn, an antiferromagnetic ring with a ground-state spin of $S=1$, and in a frustrated Cu$_3$ triangle, both with coefficients of about $2~\mathrm{rad}\, \mathrm{s}^{-1} / \mathrm{V} \mathrm{m}^{-1}$. Conversely, the antiferromagnetic ring Cr$_7$Ni, isomorphic with Cr$_7$Mn but with $S=1/2$, does not exhibit a detectable effect. We propose that the spin-electric field coupling may be used for selectively controlling individual molecules embedded in nanodevices.

Abstract:

The magnetic compass sensor in night-migratory songbirds is thought to be a flavin-tryptophan radical pair formed by blue-light excitation of the protein cryptochrome-4a (Cry4a) localized in photoreceptor cells in the birds’ retinas. The effects of applied magnetic fields on the photochemistry of purified Cry4a from the migratory European robin are well characterized but it is less clear what, if anything, distinguishes the magnetic responses of the Cry4a proteins from migratory and non-migratory species. We present here a detailed study of the magnetic sensitivity of Cry4a from the non-migratory chicken. The wild-type protein is compared with two mutants in which either Arg317 or Glu320, both close to the tryptophan radical, were replaced by the amino acids Cys and Lys, respectively, found in Cry4a from robins and other night-migratory passerines. These sites had previously been identified as probably facilitating the evolution of an optimised magnetic sensor for nocturnal orientation in songbirds. Neither of these mutations was found to affect the reaction kinetics or magnetic sensitivity of the radical pairs suggesting that any differences in Cry4a between robin and chicken must stem from their ability to transmit magnetic information via protein-protein interactions. In contrast, a Trp → Phe mutation at the end of the tryptophan-tetrad electron transfer chain in both cryptochromes led to a large increase in magnetic sensitivity suggesting different sensing and signalling roles for the third and fourth tryptophans.