Mass spectrometry (MS) has been utilized in a variety of new applications in this laboratory. Small proteins react with electrophiles, and the kinetic analysis of unstable protein adducts can be measured, e.g. trichloroethylene oxide. MS can be used to determine sequences of DNA primers elongated past DNA adducts on templates, particularly in mixtures, to evaluate the nature of miscoding. MS can also be used for the sequence analysis of DNA adducts, as demonstrated for polycyclic aromatic hydrocarbons and C4' oxidation products. High-resolution (HR) MS can distinguish <sup>2</sup>H from (natural abundance) <sup>13</sup>C and was invaluable in elucidating the catalytic mechanism of P450 19A1, the steroid aromatase, as well as P450 11A1, the cholesterol side chain cleavage enzyme. Metabolomics-type approaches with HRMS have identified substrates for “orphan” P450s (e.g., 2W1, 2U1, 4X1), and HRMS has been useful in defining the location of the orphan P450 27C1 in skin. (Supported in part by NIH R01 ES02205, R01 ES010546, R01 ES026955, R37 CA090426, and R01 GM118122.)

Biochemical and toxicological applications of mass spectrometry

254th National Meeting (2017)

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