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Fourier transform Raman spectroscopy of carcinogenic polycyclic aromatic hydrocarbons in biological systems: binding to heme proteins by H.-P. Chiang; R. Song; B. Mou; K. P. Li; P. Chiang; D. Wang; W. S. Tse; L. T. Ho is a Chemistry article available to read on EtoBox.

What is Fourier transform Raman spectroscopy of carcinogenic polycyclic aromatic hydrocarbons in biological systems: binding to heme proteins about?

The conformation of the activated complex often has a great impact on the structure 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 carcinogenesis of polycyclic aromatic hydrocarbons (PAHs), hemoglobin is employed as a model compound to simulate the heme-O 2 -PAH complex for PAH oxygenation by cytochrome P450. The Raman spectra of benzo[a]pyrene (BaP), a typical carcinogenic PAH, were acquired under different conditions and analyzed. It appears that CH wagging and ring stretching mixed strongly with CH in-plane bending are the most significantly affected vibrations. These vibrations will serve as the basis for future theoretical simulation of the complex configurations.

Who reads Fourier transform Raman spectroscopy of carcinogenic polycyclic aromatic hydrocarbons in biological systems: binding to heme proteins?

Author

H.-P. Chiang; R. Song; B. Mou; K. P. Li; P. Chiang; D. Wang; W. S. Tse; L. T. Ho

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0377-0486)

Published

1999

Language

EN

Field

Chemistry (Physical Sciences)