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- W2161929344 endingPage "1364" @default.
- W2161929344 startingPage "1351" @default.
- W2161929344 abstract "Charge transport and catalysis in enzymes often rely on amino acid radicals as intermediates. The generation and transport of these radicals are synonymous with proton-coupled electron transfer (PCET), which intrinsically is a quantum mechanical effect as both the electron and proton tunnel. The caveat to PCET is that proton transfer (PT) is fundamentally limited to short distances relative to electron transfer (ET). This predicament is resolved in biology by the evolution of enzymes to control PT and ET coordinates on highly different length scales. In doing so, the enzyme imparts exquisite thermodynamic and kinetic controls over radical transport and radical-based catalysis at cofactor active sites. This discussion will present model systems containing orthogonal ET and PT pathways, thereby allowing the proton and electron tunnelling events to be disentangled. Against this mechanistic backdrop, PCET catalysis of oxygen–oxygen bond activation by mono-oxygenases is captured at biomimetic porphyrin redox platforms. The discussion concludes with the case study of radical-based quantum catalysis in a natural biological enzyme, class I Escherichia coli ribonucleotide reductase. Studies are presented that show the enzyme utilizes both collinear and orthogonal PCET to transport charge from an assembled diiron-tyrosyl radical cofactor to the active site over 35 Å away via an amino acid radical-hopping pathway spanning two protein subunits." @default.
- W2161929344 created "2016-06-24" @default.
- W2161929344 creator A5000748653 @default.
- W2161929344 creator A5024009979 @default.
- W2161929344 creator A5056442308 @default.
- W2161929344 creator A5079771199 @default.
- W2161929344 date "2006-07-17" @default.
- W2161929344 modified "2023-10-02" @default.
- W2161929344 title "Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology" @default.
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