Uniquely in ${\mathrm{Cu}}_2{\mathrm{OSeO}}_3$, the Skyrmions, which are topologically protected magnetic spin vortexlike objects, display a magnetoelectric coupling and can be manipulated by externally applied electric ($E$) fields. Here, we explore the $E$-field coupling to the magnetoelectric Skyrmion lattice phase, and study the response using neutron scattering. Giant $E$-field induced rotations of the Skyrmion lattice are achieved that span a range of $\sim 25°$. Supporting calculations show that an $E$-field-induced Skyrmion distortion lies behind the lattice rotation. Overall, we present a new approach to Skyrmion control that makes no use of spin-transfer torques due to currents of either electrons or magnons.

In natural habitats, plants frequently experience rapid changes in the intensity of sunlight. To cope with these changes and maximize growth, plants adjust photosynthetic light utilization in electron transport and photoprotective mechanisms. This involves a proton motive force (PMF) across the thylakoid membrane, postulated to be affected by unknown anion (Cl⁻) channels. Here we report that a bestrophin-like protein from Arabidopsis thaliana functions as a voltage-dependent Cl⁻ channel in electrophysiological experiments. AtVCCN1 localizes to the thylakoid membrane, and fine-tunes PMF by anion influx into the lumen during illumination, adjusting electron transport and the photoprotective mechanisms. The activity of AtVCCN1 accelerates the activation of photoprotective mechanisms on sudden shifts to high light. Our results reveal that AtVCCN1, a member of a conserved anion channel family, acts as an early component in the rapid adjustment of photosynthesis in variable light environments.

Significance: Oxygenic photosynthesis regulates light–energy conversion by balancing the activity of the two photosystems (PSs). Such a power balance requires a sophisticated regulatory mechanism called state transitions, which involve reversible phosphorylation of the light-harvesting complex proteins (LHCIIs) to redistribute absorbed excitation energy between the two photosystems. Using noninvasive techniques (small-angle neutron scattering, circular dichroism, and absorption transient spectroscopy) in the green alga Chlamydomonas reinhardtii , we have revealed that state transitions modify the chloroplast structure, affecting the stacking and periodicity of the photosynthetic membranes and altering protein–protein interactions within these membranes. These structural changes accompany the conversion of LHCII into an energy-dissipating mode with only minor displacements of phosphorylated LHCIIs from PSII to PSI, thereby allowing us to reevaluate the physiological significance of state transitions.