Cage escape competes with geminate recombination during alkane hydroxylation by the diiron oxygenase AlkB

Rachel N. Austin, Kate Luddy, Karla Erickson, Marilla Pender-Cudlip, Erin Bertrand, Dayi Deng, Ryan S. Buzdygon, Jan B. Van Beilen, John Taylor Groves

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

(Chemical Presented) AlkBstops 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.

Original languageEnglish (US)
Pages (from-to)5232-5234
Number of pages3
JournalAngewandte Chemie - International Edition
Volume47
Issue number28
DOIs
StatePublished - Jun 27 2008

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

Keywords

  • Alkanes
  • Cytochrome AlkB
  • Oxygenases
  • Radical clocks
  • Reaction mechanisms

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    Austin, R. N., Luddy, K., Erickson, K., Pender-Cudlip, M., Bertrand, E., Deng, D., Buzdygon, R. S., Van Beilen, J. B., & Groves, J. T. (2008). Cage escape competes with geminate recombination during alkane hydroxylation by the diiron oxygenase AlkB. Angewandte Chemie - International Edition, 47(28), 5232-5234. https://doi.org/10.1002/anie.200801184