Using resonance Raman cross-section data to estimate the spin state populations of Cytochromes P450.

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 (LS) to high-spin (HS), 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 (I_LS) and (I_HS) relative to an internal standard (sodium sulfate) yield relative populations for the two spin s

SUBMITTER: Mak PJ 

PROVIDER: S-EPMC3891783 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature