Copper-dioxygen (CuO2) adducts are frequently proposed as intermediates in enzymes, yet their electronic and vibrational structures have not always been understood. [Cu(eta1-O2)TMG3tren]+ (TMG3tren = 1,1,1-tris{2-[N2-(1,1,3,3-tetramethylguanidino)]ethyl}amine) features end-on (eta1) O2 coordination in the solid state. Described here is an investigation of the compound's solution properties by nuclear magnetic resonance spectroscopy, density functional calculations, and oxygen isotope effects. The study yields two major findings. First, [Cu(eta1-O2)TMG3tren]+ is paramagnetic due to a triplet electronic structure; this is in contrast to other copper compounds where O2 is bound in a side-on manner. Second, the oxygen equilibrium isotope effect upon O2 binding to copper(I) (18O EIE [triple bond] K(16O16O)/K(16O18O) = 1.0148 +/- 0.0012) is significantly larger than those determined for iron and cobalt eta1-O2 adducts. This result is suggested to reflect greater ionic (CuII-O2-I) character within the valence bond description. A revised interpretation of the physical origins of the 18O EIEs upon O2 binding to redox metals is also advanced along with experimental data that should be used as benchmarks for interpreting 18O kinetic isotope effects upon enzyme reactions.

We report a comparative study of isolated Fe II , iron oxide particles, and metallic nanoparticles on silica for non-oxidative propane dehydrogenation. It was found that the most selective catalyst was an isolated Fe II species on silica prepared by grafting the open cyclopentadienide iron complex, bis(2,4-dimethyl-1,3-pentadienide) iron(II) or Fe(oCp) 2 . The grafting and evolution of the surface species was elucidated by 1 H NMR, diffuse reflectance infrared Fourier transform spectroscopy and X-ray absorption spectroscopies. The oxidation state and local structure of surface Fe were characterized by X-ray absorption near-edge structure (XANES) and extended X-ray absorption fine structure. The initial grafting of iron proceeds by one surface hydroxyl Si−OH reacting with Fe(oCp) 2 to release one diene ligand (oCpH), generating a SiO 2 -bound Fe II (oCp) species, 1-FeoCp. Subsequent treatment with H 2 at 400 °C leads to loss of the remaining diene ligand and formation of nanosized iron oxide clusters, 1-C. Dispersion of these Fe oxide clusters occurs at 650 °C, forming an isolated, ligand-free Fe II on silica, 1-Fe II , which is catalytically active and highly selective (∼99%) for propane dehydrogenation to propene. Under reaction conditions, there is no evidence of metallic Fe by in situ XANES. For comparison, metallic Fe nanoparticles, 2-NP-Fe 0 , were independently prepared by grafting Fe[N(SiMe 3 ) 2 ] 2 onto silica, 2-FeN*, and reducing it at 650 °C in H 2 . The Fe NPs were highly active for propane conversion but showed poor selectivity (∼14%) to propene. Independently prepared Fe oxide clusters on silica display a low activity. The sum of these results suggests that selective propane dehydrogenation occurs at isolated Fe II sites.

Copper and topaquinone (TPQ) containing amine oxidases utilize O2 for the metabolism of biogenic amines while concomitantly generating H2O2 for use by the cell. The mechanism of O2 reduction has been the subject of long-standing debate due to the obscuring influence of a proton-coupled electron transfer between the tyrosine-derived TPQ and copper, a rapidly established equilibrium precluding assignment of the enzyme in its reactive form. Here, we show that substrate-reduced pea seedling amine oxidase (PSAO) exists predominantly in the Cu(I), TPQ semiquinone state. A new mechanistic proposal for O2 reduction is advanced on the basis of thermodynamic considerations together with kinetic studies (at varying pH, temperature, and viscosity), the identification of steady-state intermediates, and the analysis of competitive oxygen kinetic isotope effects, (18)O KIEs, [kcat/KM((16,16)O2)]/[kcat/KM((16,18)O2)]. The (18)O KIE = 1.0136 +/- 0.0013 at pH 7.2 is independent of temperature from 5 degrees C to 47 degrees C and insignificantly changed to 1.0122 +/- 0.0020 upon raising the pH to 9, thus indicating the absence of kinetic complexity. Using density functional methods, the effect is found to be precisely in the range expected for reversible O2 binding to Cu(I) to afford a superoxide, [Cu(II)(eta(1)-O2)(-I)](+), intermediate. Electron transfer from the TPQ semiquinone follows in the first irreversible step to form a peroxide, Cu(II)(eta(1)-O2)(-II), intermediate driving the reduction of O2. The similar (18)O KIEs reported for copper amine oxidases from other sources raise the possibility that all enzymes react by related inner-sphere mechanisms although additional experiments are needed to test this proposal.