Taking enantiomers for a spin: There are two common ways to distinguish mirror-image molecules, or enantiomers. The first relies on their distinct interactions with circularly polarized light, the second on their interactions with a pure enantiomer of some other molecule. Now Banerjee-Ghosh et al. report a conceptually different approach to chiral resolution. Experiments showed that, depending on the direction of magnetization, chiral oligopeptides, oligonucleotides, and amino acids have enantiospecific differences in initial adsorption rates on ferromagnetic surfaces. This effect is attributed to enantiospecific induced spin polarization. Science , this issue p. 1331

This review highlights recent experimental findings related to the chirality-induced spin selectivity effect. This effect is demonstrated to explain asymmetric electron's spin transport in chiral molecules for various technological applications.

Spin-polarized catalysts have garnered significant interest in electrocatalysis, namely in the electrocatalytic oxidation of water, which has very sluggish kinetics due to its high overpotential.

Protein function may be modulated by an event occurring far away from the functional site, a phenomenon termed allostery. While classically allostery involves conformational changes, we recently observed that charge redistribution within an antibody can also lead to an allosteric effect, modulating the kinetics of binding to target antigen. In the present work, we study the association of a polyhistidine tagged enzyme (phosphoglycerate kinase, PGK) to surface-immobilized anti-His antibodies, finding a significant Charge-Reorganization Allostery (CRA) effect. We further observe that PGK’s negatively charged nucleotide substrates modulate CRA substantially, even though they bind far away from the His-tag–antibody interaction interface. In particular, binding of ATP reduces CRA by more than 50%. The results indicate that CRA is affected by the binding of charged molecules to a protein and provide further insight into the significant role that charge redistribution can play in protein function.

Considerable electric fields are present within living cells, and the role of bioelectricity has been well established at the organismal level. Yet much remains to be learned about electric-field effects on protein function. Here, we use phototriggered charge injection from a site-specifically attached ruthenium photosensitizer to directly demonstrate the effect of dynamic charge redistribution within a protein. We find that binding of an antibody to phosphoglycerate kinase (PGK) is increased twofold under illumination. Remarkably, illumination is found to suppress the enzymatic activity of PGK by a factor as large as three. These responses are sensitive to the photosensitizer position on the protein. Surprisingly, left (but not right) circularly polarized light elicits these responses, indicating that the electrons involved in the observed dynamics are spin polarized, due to spin filtration by protein chiral structures. Our results directly establish the contribution of electrical polarization as an allosteric signal within proteins. Future experiments with phototriggered charge injection will allow delineation of charge rearrangement pathways within proteins and will further depict their effects on protein function.

Augmentation of the electrocatalytic activity of a sulfur-doped Ni, Fe-containing layered double hydroxide for the oxygen evolution reaction using chiral supramolecular polymer functionalization through chiral induced spin selectivity (CISS).