Home Prof. Newcomb Research Group Research Projects Facilities Publications
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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
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Cytochrome P450
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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
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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.
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Facilities
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What's New?
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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. |
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- 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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