Cage Escape Competes with Geminate Recombination during Alkane Hydroxylation by the Diiron Oxygenase AlkB

AlkB stops the radical clock: Three structurally analogous radical‐clock substrates with a large span in their rearrangement rates are hydroxylated by AlkB to afford similar amounts of rearranged (2) and unrearranged products (1). Such a result is in accord with radical rebound competing with cage e...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2008-01, Vol.47 (28), p.5232-5234
Main Authors: Austin, Rachel N, Luddy, Kate, Erickson, Karla, Pender-Cudlip, Marilla, Bertrand, Erin, Deng, Dayi, Buzdygon, Ryan S, van Beilen, Jan B, Groves, John T
Format: Article
Language:English
Subjects:
alkanes
Alkanes - chemistry
cytochrome AlkB
Hydroxylation
Kinetics
Mixed Function Oxygenases - metabolism
oxygenases
Pseudomonas putida - enzymology
radical clocks
reaction mechanisms
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Summary:AlkB stops the radical clock: Three structurally analogous radical‐clock substrates with a large span in their rearrangement rates are hydroxylated by AlkB to afford similar amounts of rearranged (2) and unrearranged products (1). Such a result is in accord with radical rebound competing with cage escape of the geminate substrate radical. The results show that radical clocks can measure both the radical lifetime and the kinetics of cage escape.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200801184