In phytochrome Agp2 ultrafast proton-transfer occurs from the chromophore to a hydrogen-bonded water network in the protein prior to photoisomerization. The altered hydrogen bonds persist after photoisomerization and trigger together with the new chromophore geometry the activated protein conformation.

We have unearthed a new artificial organelle known as “Concentriosome” to carry out spatiotemporal enzymatic cascade reactions in solution and regiospecific chemical events using the standing waves that in turn are generated by the Faraday Instability setup.

The design, synthesis, and high-resolution single-crystal X-ray structure of a superfluorinated 20 kDa gold nanocluster was achieved. The nanocluster presents an Au25 core coated by a shell of multi-branched highly fluorinated thiols (SF27) resulting in almost 500 fluorine atoms.

Engineering enzymes with new-to-nature reactivity remains a great challenge in biocatalysis. Combining the merits of biocatalysis and photocatalysis represents a powerful approach to address this challenge.

We report a strategy to control enzyme-mediated cascade reactions within audible sound-induced transient domains created in a solution.

Homogeneous photocatalysis typically employs one-photon-absorbing photosensitizers and requires UV/visible light irradiation. Herein, we report a group of ruthenium complexes with two-photon-absorption capabilities to drive organic photocatalysis using low-cost NIR LED (740 nm) as the light source.