Oxygen atom transfer in models for molybdenum enzymes: isolation and structural, spectroscopic, and computational studies of intermediates in oxygen atom transfer from molybdenum(VI) to phosphorus(III).

Intermediates in the oxygen atom transfer from Mo(VI) to P(III), [Tp(iPr)MoOX(OPR3)] (Tp(iPr) = hydrotris(3-isopropylpyrazol-1-yl)borate; X = Cl-, phenolates, thiolates), have been isolated from the reactions of [Tp(iPr)MoO2X] with phosphines (PEt3, PMePh2, PPh3). The green, diamagnetic oxomolybdenum(IV) complexes possess local C(1) symmetry (by NMR spectroscopy) and exhibit IR bands assigned to nu(Mo==O) (approximately 950 cm(-1)) and nu(P==O) (1140-1083 cm(-1)) vibrations. The X-ray crystal structures of [Tp(iPr)MoOX(OPEt3)] (X = OC6H4-2-sBu, SnBu), [Tp(iPr)MoO(OPh)(OPMePh2)], and [Tp(iPr)MoOCl(OPPh3)] have been determined. The monomeric complexes exhibit distorted octahedral geometries, with coordination spheres composed of tridentate fac-Tp(iPr) and mutually cis monodentate terminal oxo, phosphoryl (phosphine oxide), and monoanionic X ligands. The electronic structures and stabilities of the complexes have been probed by computational methods, with the three-dimensional energy surfaces confirming the existence of a low-energy steric pocket that restricts the conformational freedom of the phosphoryl ligand and inhibits complete oxygen atom transfer. The reactivity of the complexes is also briefly described.