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.) 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
Language:	English
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
Online Access:	Get full text
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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. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200801184