Resonance Raman Spectroscopy of the Oxygenated Intermediates of Human CYP19A1 Implicates a Compound I Intermediate in the Final Lyase Step
Document Type
Article
Language
eng
Format of Original
4 p.
Publication Date
4-2-2014
Publisher
American Chemical Society
Source Publication
Journal of the American Chemical Society
Source ISSN
0002-7863
Original Item ID
DOI: 10.1021/ja500054c
Abstract
CYP19A1, or aromatase, a cytochrome P450 responsible for estrogen biosynthesis in humans, is an important therapeutic target for the treatment of breast cancer. There is still controversy surrounding the identity of reaction intermediate that catalyzes carbon–carbon scission in this key enzyme. Probing the oxy-complexes of CYP19A1 poised for hydroxylase and lyase chemistries using resonance Raman spectroscopy and drawing a comparison with CYP17A1, we have found no significant difference in the frequencies or isotopic shifts for these two steps in CYP19A1. Our experiments implicate the involvement of Compound I in the terminal lyase step of CYP19A1 catalysis.
Recommended Citation
Mak, Piotr J.; Luthra, Abhinav; Sligar, Stephen G.; and Kincaid, James R., "Resonance Raman Spectroscopy of the Oxygenated Intermediates of Human CYP19A1 Implicates a Compound I Intermediate in the Final Lyase Step" (2014). Chemistry Faculty Research and Publications. 361.
https://epublications.marquette.edu/chem_fac/361
Comments
Published version. Journal of the American Chemical Society, Vol. 136, No. 13 (April 2014): 4825-4828. DOI. © 2014 American Chemical Society. Used with permission.
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