The reaction of alternate oxidants with cytochrome P450BM3 and mutants generates spectrally detectable, high valent iron intermediates

UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
Jonathan Ira Thompson (Creator)
The University of North Carolina at Greensboro (UNCG )
Web Site:
Gregory Raner

Abstract: "The Cytochrome P450 family serves as the forefront for xenobiotic metabolism in the human body. An understanding of the mechanism behind this enzyme family is a necessity for later research in the areas of pharmaceuticals and biochemistry. It has been observed by previous researchers that the transient species compound I, a highly reactive π-cation radical intermediate, is able to be viewed with P450cam and other heme containing proteins with subjection to various oxidant compounds such as m-CPBA or peracetic acid. In this study Cytochrome P450BM3 and its' heme domain, P450BMH, has been reacted with various oxidant compounds to show evidence of this compound I intermediate by diode array spectrophotometry and electron paramagnetic resonance spectroscopy."--Abstract from author supplied metadata.

Additional Information

Language: English
Date: 2006
Cytochrome P450, xenobiotic metabolism, pharmaceuticals, biochemistry
Cytochrome P-450

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