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https://www.selleckchem.com/products/folinic-acid.html Expanding the reaction scope of natural metalloenzymes can provide new opportunities for biocatalysis. Mononuclear non-heme iron-dependent enzymes represent a large class of biological catalysts involved in the biosynthesis of natural products and catabolism of xenobiotics, among other processes. Here, we report that several members of this enzyme family, including Rieske dioxygenases as well as α-ketoglutarate-dependent dioxygenases and halogenases, are able to catalyze the intramolecular C-H amination of a sulfonyl azide substrate, thereby exhibiting a promiscuous nitrene transfer reactivity. One of these enzymes, naphthalene dioxygenase (NDO), was further engineered resulting in several active site variants that function as C-H aminases. Furthermore, this enzyme could be applied to execute this non-native transformation on a gram scale in a bioreactor, thus demonstrating its potential for synthetic applications. These studies highlight the functional versatility of non-heme iron-dependent enzymes and pave the way to their further investigation and development as promising biocatalysts for non-native metal-catalyzed transformations. © 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.The first example of CO 2 -responsive spin state conversion between high-spin (HS) and low-spin (LS) states at room temperature was achieved in a monomeric cobalt(II) complex. A neutral cobalt(II) complex, [Co II (COO-terpy) 2 ]·4H 2 O ( 1·4H 2 O ), stably formed cavities generated via π-π stacking motifs and hydrogen bond networks, resulted in the accommodation of four water molecules. A crystalline 1·4H 2 O transformed to the solvent-free 1 without loss of the porosity by heating up to 420 K. Compound 1 exhibited a selective carbon dioxide (CO 2 ) adsorption via a gate-open type of the structural modification. Furthermore, the HS/LS transition temperature ( T 1/2 ) was able to be tuned by the CO 2 -pressure over a wide temperature

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