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A series of bioinspired dioxidomolybdenum(VI), dioxidotungsten(VI) and oxidovanadium(V) complexes [MoO2(H2L Saltris )], [WO2(H2L Saltris )] and [VO(HL Saltris )]2 were prepared by the reaction of a hydroxyl-rich Schiff base proligand N-(1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl)-3,5-di-tert-butylsalicylaldimine (H4L Saltris ) with metal precursors in methanol solutions. Molybdenum and tungsten complexes crystallize as mononuclear molecules, whereas the vanadium complex forms dinuclear units. From the complexes, [VO(HL Saltris )]2 shows activity in the oxidation of 4-tert-butylcatechol and 3,5di-tert-butylcatechol, mimicking the action of the dicopper enzyme catechol oxidase. *

Six known aminophenolate vanadium complexes V1–V6 were examined in 3,5-di-tert-butylcatechol (1, 3,5-DTBC) oxidation. From the complexes V1–V5 have been previously shown to demonstrate catechol oxidase-like (catecholase) behaviour, catalytically oxidizing 1...

L-proline was used to prepare chiral, tridentate amino acid phenol proligands H2L [1][2][3][4] . These proligands react with vanadium precursors VO(acac)2, VOSO4 • 5 H2O and VO(OPr)3 in methanol to form the corresponding oxidoalkoxidovanadium(V) complexes 1-4. The complexes crystallize from methanol, and are octahedrally coordinated with a general formula [VO(L 1-4 )(OMe)(MeOH)]. In solution, however, they adopt several different conformations or isomeric structures depending on the solvent. Highlights• Tridentate amino acid phenol proligands were made of L-proline.• Proligands react with various vanadium precursors to form oxidoalkoxidovanadium(V) complexes. • In solution, the complexes adopt different conformations or isomeric structures.• The solid-state structures resemble the active site found in vanadium bromoperoxidase.

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