Fourier transform Raman spectroscopy of carcinogenic polycyclic aromatic hydrocarbons in biological systems: Binding to heme proteins

Citation
Hp. Chiang et al., Fourier transform Raman spectroscopy of carcinogenic polycyclic aromatic hydrocarbons in biological systems: Binding to heme proteins, J RAMAN SP, 30(7), 1999, pp. 551-555
Citations number
32
Categorie Soggetti
Spectroscopy /Instrumentation/Analytical Sciences
Journal title
JOURNAL OF RAMAN SPECTROSCOPY
ISSN journal
03770486 → ACNP
Volume
30
Issue
7
Year of publication
1999
Pages
551 - 555
Database
ISI
SICI code
0377-0486(199907)30:7<551:FTRSOC>2.0.ZU;2-6
Abstract
The conformation of the activated complex often has a great impact on the s tructure of reaction products. It is an essential piece of information for a better understanding of reaction mechanisms at the molecular level. Among all analytical methods, Raman spectroscopy is perhaps the most convenient to provide such information. To elucidate the molecular mechanisms of the c arcinogenesis of polycyclic aromatic hydrocarbons (PAHs), hemoglobin is emp loyed as a model compound to simulate the heme-O-2-PAH complex for PAH oxyg enation by cytochrome P450, The Raman spectra of benzo[a]pyrene (BaP), a ty pical carcinogenic PAH, were acquired under different conditions and analyz ed. It appears that CH wagging and ring stretching mixed strongly with CH i n-plane bending are the most significantly affected vibrations, These vibra tions will serve as the basis for future theoretical simulation of the comp lex configurations. Copyright (C) 1999 John Wiley & Sons, Ltd.