Research on Some Aspects of the Cytochrome P450 Proteins

Abstract

The Cytochrome P450 was first described in 1958 as a brown pigment when carbon monoxide was added to hepatic microsomal preparations, which had been reduced with dithionite or NADH. This hemeprotein had probably arisen very early in chemical evolution (the origin of life). One of its early functions was probably the detoxification of molecular oxygen, which was poisonous to primordial life, which had not evolved other protective mechanisms. Since its initial discovery, it has been identified in a very large variety of animal tissues, plants and microorganisms. It is now known that there are various cytochromes P450, which perform a large variety of enzymatic functions. The cytochromes P450 have among other functions the metabolism or detoxification of ‘xenobiotics’ or ‘foreign chemicals’, which include drugs and environmental pollutants. The functioning of the steroid hydroxylases in adrenocortical mitochondria is influenced (regulated) by the dielectric constant in the immediate vicinity of the enzyme. Sodium and potassium ions influence the functioning of these hydroxylases differently in view of the different effect their ionic radii have on the dielectric constant. Spices have been found to bind to cytochrome P450. This may modify the activity of the enzyme. This may account for certain herbal medicinal preparations being effective in members of some communities but not in others, which have different dietary habits or preparations. Spices are also added as a component of some herbal medicinal preparations. More investigations need to be performed to ascertain the effect the consumption of spices may have on the efficacy of medicines in general.