Narrow Results

Cyclodextrins are versatile building blocks for a variety of macromolecules due to the inclusion complexes that are formed with hydrophobic organic molecules. Cyclodextrin-porphyrin interactions are of particular interest since cyclodextrins can serve as a non-covalent binding pocket while metalloporphyrins could serve as the heme analogs in the construction of heme protein model compounds. Various approaches to the design and assembly of biomimetic porphyrin constructs are compared and contrasted in this minireview with a particular emphasis on self-assembled and porphyrin-cyclodextrin systems. Several recent advances from our laboratories are described in this context. A sensitive fluorescent binding probe, 6^A-N-dansyl-permethylated-β-cyclodextrin (Dan-NH-TMCD), was found to form 2:1 complexes with the meso-tetraphenylporphyrins Mn(III)TCPP, Mn(III)TPPS and Mn(III)TF₄TMAP with high binding constants. A perPEGylated cyclodextrin, heptakis(2,3,6-tri-O-2-(2-(2-methoxyethoxy)ethoxy)ethyl)-β-cyclodextrin (TPCD), has been shown by ¹H NMR spectroscopy to form a 1:1 complex with H₂TCPP with a binding constant above 10⁸M^-1. Such a strong binding constant is the largest found for a 1:1 complex between a monomeric cyclodextrin and a guest. TPCD was also found to bind Mn(III)TCPP with a binding constant of 1.2 × 10⁶M^-1. A novel, self-assembled hemoprotein model, hemodextrin is also described. The molecular design is based on a PEGylated cyclodextrin scaffold that bears both a heme-binding pocket and an axial ligand that binds an iron porphyrin. The binding constant for Fe(III)TPPS (iron(III) meso-tetra(4-sulfonatophenyl)porphyrin) by py-PPCD was determined to be 2 × 10⁶M^-1. The pyridyl nitrogen of py-PPCD was shown to ligate to the iron center by observing signal changes in the Fe(II)-porphyrin ¹H NMR spectrum. This hemodextrin ensemble, a minimalist myoglobin, was shown to bind dioxygen reversibly and to form a stable ferryl species.

A novel industrial-scale trial for cyclohexane oxidation with air over metalloporphyrins as cytochrome P-450 monooxygenase model was reported. Upon addition of extremely low concentrations (1–5 ppm) of simple cobalt porphyrin to the commercial cyclohexane oxidation system, and decrease of the reaction temperature and pressure about 20 °C and 0.4 MPa respectively, the conversion rate of the cyclohexane oxidation increased from 4.8% to 7.1%, the yield of cyclohexanone raised from 77% to 87%, and a 70,000-ton cyclohexanone equipment set yielded an output of 125,000 tons cyclohexanone. Furthermore, a novel biological-chemical-cycle coupling mechanism was proposed to rationalize the aerobic oxidations of hydrocarbons catalyzed by the metalloporphyrins.