Abstract
Surface-enhanced Raman scattering was used as a spectroscopic tool to investigate the changes brought upon cytochrome P450BSss after fatty acid binding. Differences in the spectra of substrate-free and substrate-bound enzyme were observed indicating the potential for this method to be used in the screening of P450 substrates. In particular, the binding characteristics of myristic acid, an inherent substrate, and hydroxylauric acid, a product of fatty acid oxidation, towards P450BSss in the presence of H(2)O(2) were investigated. Specific spectral changes could be assigned to changes in the heme environment only for myristic acid, indicating an occurrence of oxidation process characteristic for the enzymatic substrate.
Published Version
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