Artificial metalloenzymes result from anchoring an organometallic catalyst within evolvable protein scaffold. Thanks to its dimer of dimers quaternary structure, streptavidin allows the precise positioning two metal cofactors activate a single substrate, thus expanding reaction scope accessible artificial metalloenzymes. To validate this concept, we report herein on our efforts engineer and evo...

We report on our efforts to create efficient artificial metalloenzymes for the enantioselective hydrogenation of N-protected dehydroamino acids using either avidin or streptavidin as host proteins. Introduction of chiral amino acid spacers – phenylalanine or proline – between the biotin anchor and the flexible aminodiphosphine moiety 1, combined with saturation mutagenesis at position S112X of ...

Incorporation of a biotinylated Hoveyda-Grubbs catalyst within (strept)avidin affords artificial metalloenzymes for the ring-closing metathesis of N-tosyl diallylamine in aqueous solution. Optimization of the performance can be achieved either by chemical or genetic means.

Incorporation of biotinylated-[rhodium(diphosphine)]+ complexes, with enantiopure amino acid spacers, in streptavidin affords solvent-tolerant and selective artificial metalloenzymes: up to 91% ee (S) in the hydrogenation of N-protected dehydroamino acids.

In this paper a novel kind of fluxgate is presented. The sensor is based on helical anisotropy of the ferromagnetic layer, electrodeposited on cupper wire. The saturating field is provided by current flowing in the wire, and the output voltage is measured directly at the terminations of the wire. Therefore no coils are necessary, making possible high miniaturization of the sensor. The effect ha...