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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Published inAngewandte Chemie (International ed.) Vol. 47; no. 28; pp. 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 Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 01.01.2008
WILEY-VCH Verlag
WILEY‐VCH Verlag
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.
Bibliography:http://dx.doi.org/10.1002/anie.200801184
We thank FMC, Princeton, for access to GC-MS instrumentation and NSF (CHE-0221978 (R.N.A., J.T.G.) and CHE 0616633 (J.T.G.)), NIH (GM 072506 (R.N.A.) and 2R37M036298 (J.T.G.)), the Henry Dreyfus Foundation (R.N.A.), and the Howard Hughes Foundation (R.N.A.) for support of this work.
istex:D1BDE5AAA18E33E87A9B399FC2EFEC1FCA8A93C1
NIH - No. GM 072506; No. 2R37M036298
Howard Hughes Foundation
ArticleID:ANIE200801184
NSF - No. CHE-0221978; No. CHE 0616633
ark:/67375/WNG-7ZKD9G6W-5
Henry Dreyfus Foundation
We thank FMC, Princeton, for access to GC‐MS instrumentation and NSF (CHE‐0221978 (R.N.A., J.T.G.) and CHE 0616633 (J.T.G.)), NIH (GM 072506 (R.N.A.) and 2R37M036298 (J.T.G.)), the Henry Dreyfus Foundation (R.N.A.), and the Howard Hughes Foundation (R.N.A.) for support of this work.
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200801184