Conformational change of cytochrome P450 1A2 induced by sodium chloride.

Recently, it was reported that the activity of rabbit P450 1A2 is markedly increased at elevated sodium phosphate concentration. Here, the possible structural change of rabbit P450 1A2 accompanying the NaCl-induced increase in its enzyme activity is investigated by fluorescence spectroscopy, circular dichroism, and absorption spectroscopy. It was found that NaCl increased alpha-helix content and lowered beta-sheet content of P450 1A2 in the presence as well as in the absence of a phospholipid. Intrinsic fluorescence emissions also increased with increasing NaCl concentration. The low spin iron configuration of P450 1A2 shifted toward the high spin configuration in response to the increased salt concentration. The effect of increased potassium phosphate and NaCl on the P450 1A2 activity was also studied. It was found that the activity increase of rabbit P450 1A2 occurs concomitantly with the conformational change including raised alpha-helix content.