Efficient conversion of alkenes to chlorohydrins by a Ru-based artificial enzyme.

Artificial enzymes are required to catalyse non-natural reactions. Here, a hybrid catalyst was developed by embedding a novel Ru complex in the transport protein NikA. The protein scaffold activates the bound Ru complex to produce a catalyst with high regio- and stereo-selectivity.

Vanadium thiolate complexes for efficient and selective sulfoxidation catalysis: a mechanistic investigation.

The structural and electronic properties as well as the catalytic activity toward sulfoxidation of two new vanadium complexes have been investigated. They both possess in their coordination sphere two alkyl thiolate ligands: a dioxido V(V) complex [VO2L(NS2)](HNEt3) (1) (L(NS2) = 2,2'-(pyridine-2,6-diyl)bis(1,1'-diphenylethanethiol)) and an oxido V(IV) complex [VOL(N2S2)] (2) (L(N2S2) = 2,2'-(2,2'-bipyridine-6,6'-diyl)bis(1,1'-diphenylethanethiol)). The X-ray structure of 1 has revealed that the V(V) metal ion is at the center of a distorted trigonal bipyramid.

The protein environment drives selectivity for sulfide oxidation by an artificial metalloenzyme.

MAGIC Mn-salen mETALLOZYME: The design of an original, artificial, inorganic, complex-protein adduct, has led to a better understanding of the synergistic effects of both partners. The exclusive formation of sulfoxides by the hybrid biocatalyst, as opposed to sulfone in the case of the free inorganic complex, highlights the modulating role of the inorganic-complex-binding site in the protein. Artificial metalloenzymes based on the incorporation of Mn-salen complexes into human serum albumin display high efficiency and selectivity for sulfoxide production during sulfide oxidation.

A new chiral diiron catalyst for enantioselective epoxidation.

The dinuclear chiral complex Fe(2)O(bisPB)(4)(X)(2)(ClO(4))(4) (X = H(2)O or CH(3)CN) catalyzes with high efficiency (up to 850 TON) and moderate enantioselectivity (63%) the epoxidation of electron deficient alkenes at 0 degrees C by a peracid.