Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Radicals in enzymatic reactions

P A Frey1

  • 1Institute for Enzyme Research, University of Wisconsin-Madison, 1710 University Avenue, Madison, WI 53705, USA. frey@enzyme.wisc.edu

Current Opinion in Chemical Biology
|July 17, 1998
PubMed
Summary

Recent studies show substrate radicals in lysine 2,3-aminomutase and methane monooxygenase reactions. This contrasts with ribonucleotide reductase, which may involve protein-based thiyl radicals, sparking debate on enzyme mechanisms.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Climate change and the integrity of science.

Science (New York, N.Y.)·2010
Same author

Pyruvate dehydrogenase complex of Escherichia coli: radial mass analysis of subcomplexes by scanning transmission electron microscopy.

Biophysical journal·2009
Same author

Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases.

Biochemistry·2006
Same author

The role of radicals in enzymatic processes.

Chemical record (New York, N.Y.)·2002
Same author

Enzymology. Coenzymes and radicals.

Science (New York, N.Y.)·2001
Same author

Radical mechanisms of S-adenosylmethionine-dependent enzymes.

Advances in protein chemistry·2001

Area of Science:

  • Biochemistry and enzymology
  • Free radical chemistry in biological systems

Background:

  • Enzyme mechanisms involving radical intermediates are crucial in biological processes.
  • Recent spectroscopic and kinetic data have illuminated radical involvement in key enzymes.
  • Specific enzymes like lysine 2,3-aminomutase, methane monooxygenase, and ribonucleotide reductase are under investigation.

Purpose of the Study:

  • To review and correlate recent evidence for substrate-based radicals in enzyme catalysis.
  • To compare proposed mechanisms involving substrate radicals with those involving protein-based radicals.
  • To address controversies surrounding the reaction mechanisms of ribonucleotide reductase and methane monooxygenase.

Main Methods:

  • Spectroscopic techniques to detect radical species.
  • Kinetic analyses to elucidate reaction pathways.
  • Comparative analysis of proposed enzymatic mechanisms.

Main Results:

  • Spectroscopic and kinetic evidence supports the presence of substrate-based radicals in lysine 2,3-aminomutase and methane monooxygenase.
  • Evidence for a protein-based thiyl radical in ribonucleotide reductase has been linked to mechanisms involving substrate radicals.
  • Discrepancies in proposed mechanisms for ribonucleotide reductase and methane monooxygenase have been highlighted.

Conclusions:

  • The findings suggest diverse radical-based mechanisms across different enzymes.
  • Further research is needed to resolve mechanistic controversies in ribonucleotide reductase and methane monooxygenase.
  • Understanding these radical pathways is key to comprehending enzyme function and evolution.

Related Experiment Videos