Abstract
This chapter discusses the chemical modification of interaction between adrenodoxin and cytochrome P450scc. Cytochrome P450scc is an integral membrane protein located in the inner membrane of adrenal cortex mitochondria that carries out the three-step oxidative side-chain cleavage of cholesterol to form pregnenolone. This chapter presents detailed chemical modification procedures to characterize the interaction between adrenodoxin and cytochrome P450scc. Methods for the specific modification of lysine, arginine, glutamate, and aspartate residues are presented, along with procedures to analyze the effects of these modifications on protein-protein interactions. The limitations and caveats of the chemical modification procedures are discussed. A number of different factors can lead to a change in protein function as a result of the chemical modification of an amino acid residue. For this reason, caution should be used in the interpretation of chemical modification experiments. It is difficult to distinguish between a direct, localized effect on function, and the effect of a global long-range change in conformation accompanying modification.
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