Use of Isotopes and Isotope Effects for Investigations of Diiron Oxygenase Mechanisms

Rahul Banerjee, Anna J. Komor, John D. Lipscomb

Research output: Chapter in Book/Report/Conference proceedingChapter

12 Scopus citations


Isotope effects of four broad and overlapping categories have been applied to the study of the mechanisms of chemical reaction and regulation of nonheme diiron cluster-containing oxygenases. The categories are: (a) mass properties that allow substrate-to-product conversions to be tracked, (b) atomic properties that allow specialized spectroscopies, (c) mass properties that impact primarily vibrational spectroscopies, and (d) bond dissociation energy shifts that permit dynamic isotope effect studies of many types. The application of these categories of isotope effects is illustrated using the soluble methane monooxygenase system and CmlI, which catalyzes the multistep arylamine to arylnitro conversion in the biosynthetic pathway for chloramphenicol.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Number of pages52
StatePublished - 2017

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Bibliographical note

Publisher Copyright:
© 2017 Elsevier Inc.


  • Arylamine oxygenase
  • Chiral ethane
  • Chloramphenicol
  • CmlI
  • Dinuclear iron cluster
  • Fe
  • Methane monooxygenase
  • Mössbauer
  • O
  • Oxygen activation
  • Rapid freeze-quench
  • Resonance Raman
  • Stopped flow


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