Epoxidation of polybutadiene by a topologically linked catalyst

Pall Thordarson, Edward J. A. Bijsterveld, Alan E. Rowan () and Roeland J. M. Nolte
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Pall Thordarson: University of Nijmegen
Edward J. A. Bijsterveld: University of Nijmegen
Alan E. Rowan: University of Nijmegen
Roeland J. M. Nolte: University of Nijmegen

Nature, 2003, vol. 424, issue 6951, 915-918

Abstract: Abstract Nature has evolved complex enzyme architectures that facilitate the synthesis and manipulation of the biopolymers DNA and RNA, including enzymes capable of attaching to the biopolymer substrate and performing several rounds of catalysis before dissociating1,2,3,4,5. Many of these ‘processive’ enzymes have a toroidal shape and completely enclose the biopolymer while moving along its chain, as exemplified by the DNA enzymes T4 DNA polymerase holoenzyme6 and λ-exonucleoase7. The overall architecture of these systems resembles that of rotaxanes, in which a long molecule or polymer is threaded through a macrocycle. Here we describe a rotaxane that mimics the ability of processive enzymes to catalyse multiple rounds of reaction while the polymer substrate stays bound. The catalyst consists of a substrate binding cavity incorporating a manganese(III) porphyrin complex that oxidizes alkenes within the toroid cavity, provided a ligand has been attached to the outer face of the toroid to both activate the porphyrin complex and shield it from being able to oxidize alkenes outside the cavity. We find that when threaded onto a polybutadiene polymer strand, this catalyst epoxidizes the double bonds of the polymer, thereby acting as a simple analogue of the enzyme systems.

Date: 2003
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DOI: 10.1038/nature01925

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