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Newcomb's Research Group

 

 

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Welcome to the group website

     Dr. Martin Newcomb is an LAS Distinguished Professor of Chemistry.  He and his group moved to the University of Illinois at Chicago in 2001.  His research focuses on several aspects of radical chemistry including ultrafast reactions and radical reactions in biological systems.

 

Research Projects

 

Cytochrome P450

     Current research projects in the group include laser flash photolysis (LFP)  kinetic studies of radical and radical cation reactions, mechanisms of cytochrome P450 and methane monooxygenase (MMO) enzyme-catalyzed oxidations, reactions of DNA and related radicals, and radical reactions catalyzed by coenzyme B-12 and S-adenosylmethionine (SAM) dependent enzymes.

     Research Projects are ongoing in the following areas.

  • New methods in Laser Flash Photolysis
  • Kinetics of enol ether radical cations
  • Cytochrome P450 and MMO
  • B-12 and SAM enzymes
       The active site of cytochrome P450(cam).  The catalyst contains heme (iron-porphyrin) with sulfur of cysteine (yellow) serving as the fifth iron ligand.  The natural substrate, camphor, is bound in the active site in this crystal structure.

     

Facilities

 

What's New?

The Newcomb group is equipped with some of the most modern tools for organic chemistry research, including laser flash photolysis kinetic spectrometers with nanosecond and picosecond lasers, automated GCs, GC-mass spec, and HPLC.  The group also has a functional biochemistry laboratory for enzyme isolation and study.  
  • Radical H-atom abstraction from Cp2TiCl-H2O complex, JOC Featured Article  jo801869r
  • P450 Compound I rate constants measured for the first time.  ja802652b
  • XAFS spectroscopy of a Cytochrome P450 Compound II derivative  pnas0708299105
  • Cytochrome P450 119 Compound I by Photo-Oxidation of Compound II  ja060048y
  • Kinetics of oxidations by Compound I of CYP2B4, a mammalian hepatic P450 and its mutants.

 

 

 

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This site was last updated 11/01/08