Mass spectrometric analysis of the heme cofactor of cytochrome P450(BM-3) in Escherichia coli HU-227 cells, and, Increasing P450 expression in HU-227 cells using transformation experiments

Cytochrome P450 is responsible for the biotransformation of various xenobiotics and endobiotics in mammals, plants and bacteria. In humans, Cytochrome P450 metabolizes a variety of pharmaceuticals on the market today. As a result, drugs are being designed and tailored to the oxygenation pathway of P450 and its substrates. However, there are a number of drug interactions as the number of new drugs on the market increase. Thus analysis of drug metabolites and intermediates are important in understanding the drug/drug interactions. X-ray crystallography has proven to be good method in analyzing P450s however, some P450s are insoluble and the resolution of intermediates is not that great. As a result NMR spectroscopy would prove to be a better method especially 13C NMR spectroscopy. 13C signals would be sensitive to the detector and would give better insight to the electronic properties in the active site of P450s and the intermediates formed in the oxygenation pathways of its substrates.