Document Type

Article

Language

eng

Format of Original

3 p.

Publication Date

12-2013

Publisher

Wiley

Source Publication

Journal of Raman Spectroscopy

Source ISSN

0377-0486

Original Item ID

DOI: 10.1002/jrs.4401

Abstract

The cytochromes P450 (CYPs) are heme proteins responsible for the oxidation of xenobiotics and pharmaceuticals and the biosynthesis of essential steroid products. In all cases, substrate binding initiates the enzymatic cycle, converting ferric low-spin to high-spin state, with the efficiency of the conversion varying widely for different substrates, so documentation of this conversion for a given substrate is an important objective. Resonance Raman (rR) spectroscopy can effectively yield distinctive frequencies for the ν3 ‘spin state marker’ bands. Here, employing a reference cytochrome P450 (CYP101), the intensities of the ν3 modes (ILS) and (IHS) relative to an internal standard (sodium sulfate) yield relative populations for the two spin states; i.e., a value of 1.24 was determined for the ratio of the relative cross sections for the ν3 modes. The use of this value was then shown to permit a reliable calculation of relative populations of the two spin states from rR spectra of several other CYPs P450. The importance of this work is that, using this information, it is now possible to conveniently document by rR the spin state population without conducting separate experiments requiring different analytical methods, instrumentation, and additional sample.

Comments

This is the peer reviewed version of the article appearing in Journal of Raman Spectroscopy, Vol. 44, No. 12 (December 2013): 1792–1794. It has been published in final form here: DOI. © 2013 Wiley. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.

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